Progress 07/01/04 to 06/23/09
Outputs
Progress Report Objectives (from AD-416) 1. Functional modification, leather and leather byproducts: Develop a foundation for the use of new chemical and biochemical technologies (a) in the production of high quality chrome-free leathers, (b) in expanding the range of high value biomaterial applications for solubilized proteins from leather byproducts. 2. Functional modification, wool: Modify wool to impart functionality for improved performance and expanded uses of domestic wool. Approach (from AD-416) 1. Collagen modification is central to both tanning and byproduct utilization. (a) To develop a basis for designing or selecting effective sustainable tanning agents, the results of theoretical and experimental model studies will be integrated to give the best overall evaluation. Targets for chrome-free tanning agents will include natural products (tannins, genipin), enzymes for protein modification (transglutaminase, oxidases), and organic chemicals (aldehydes, acrylates). (b) Gelatin byproducts from leather processing will be evaluated alone and in combination with other proteins from renewable agricultural resources as potential coatings and fillers for use in leather or wool processing. Partially hydrolyzed collagen recovered from leather waste will also be combined with fibrous protein waste products for the preparation of novel composite materials with useful properties, such as high strength and thermal stability, for use in a variety of industrial applications, such as "bonded" leather and shoe inner soles. 2. The ERRC process (patent pending) of treating wool fabric for shrinkage control will be evaluated on wool blended with other natural and synthetic fibers, and yarn-dyed fabrics. Chemical and biochemical modifications of intact wool to add functionality will be evaluated for improved properties, such as softness, comfort, resistance to shrinkage, improved flame retardancy, and resistance to photodegradation. Collagen hydrolysates, or other proteinaceous carriers, will be applied to wool fabric as a vehicle for introducing agents that impart such properties as improved whiteness, resistance to ignition, and photoprotection. Significant Activities that Support Special Target Populations 1a. In the development of a fundamental understanding of the mechanisms of tanning, computational methods developed in previous years were used to simulate interactions of a vegetable tanning material, with collagen. Both H-bonding and hydrophobic sites for the interaction of gallotannin, a model tannin, with collagen were identified, the system was simulated with and without a layer of water on the tannin molecules to evaluate hydration effects. Protocols for the production and characterization of research quantities of chrome-free powdered hide from different pretreatments were developed. Well-characterized powdered hide was used in tanning experiments with aldehyde type tanning agents to provide additional details of the mechanisms of tanning that complement the data obtained from our soluble collagen model system. 1b. For the processing of solid wastes from leather tanning into valuable products using biotechnology, chemically and enzymatically- modified biopolymers developed in previous years were applied as fillers to unfinished leathers made from poor quality, veiny or loose grained, hides to produce leathers that when finished were significantly improved over untreated leathers from the same type of hide. Cattle hides that exhibited a seasonal defect known as "spring break" were evaluated by Scanning Electron Microscopy (SEM) and X ray tomography to show for the first time that in contrast to normal hides, the fibers of these hides appeared to be compacted or cemented together. The spring break effect was most noticeable in the belly area of the hides, when this area was treated with our biopolymers and examined by SEM, the fibers appeared to be coated with biopolymer and better separated. Continued to work with industrial partner in the design of more efficient filler processes, applying basic cost analysis principles to variable parameters (time, energy, water and chemicals). 2. For the development of novel uses of existing products for unique high-value purposes, wool fibers were treated by various oxidation and reduction methods to extract keratin and produce a broad array of keratin products in the forms of powder, film, mat, hydrogel, sponge, and microfibers. The extracted keratin materials were characterized to evaluate molecular size, peptide families, and degree of native structure. These materials are biocompatible, nontoxic, and have a broad range of functionalities. They may be useful in skin creams as lubricants and wrinkle reducers and may function as replacements for petroleum-derived constituents, or to serve as carriers of active agents for delivery to wool and protein substrates. Wool fabric was improved by applications of keratin to control dimensional stability. Nanoparticle silver material was produced and its combination with keratin was demonstrated. Keratin associated silver nanoparticles showed antimicrobial efficacy for future application to wool fibers. Technology Transfer Number of New/Active MTAs(providing only): 1 Number of Invention Disclosures submitted: 1
Impacts
(N/A)
Publications
- Hernandez, E., Taylor, M.M., Phillips, J.G., Marmer, W.N., Brown, E.M. 2009.PROPERTIES OF BIOPOLYMERS PRODUCED BY TRANSGLUTAMINASE TREATMENT OF WHEY PROTEIN ISOLATE AND GELATIN. Bioresource Technology. 100(14):3638- 3643.
- Cardamone, J.M., Martin, J. 2008. Keratin Coatings for Wool: Shrinkproofing and Nanoparticle Delivery. Macromolecular Symposium. 272:161-166.
- Ding, K., Taylor, M.M., Brown, E.M. 2008. Tanning Effects of Aluminum - Genipin or -Vegetable Tannin Combinations. Journal of American Leather Chemists Association. 103(11):377-382.
- Taylor, M.M., Bumanlag, L.P., Marmer, W.N., Brown, E.M. 2009. Potential application for genipin-modified gelatin in leather processing. Journal of American Leather Chemists Association. 104(3):79-91.
- Hernandez Balada, E., Taylor, M.M., Brown, E.M., Liu, C., Cot, J. 2009. Whey Protein Isolate: A Potential Filler for the Leather Industry. Journal of American Leather Chemists Association. 104(4):122-130.
- Brown, E.M., Qi, P.X. 2008. Exploring a Role in Tanning for the Gap Region of the Collagen Fibril: Catechin-Collagen Interactions. Journal of American Leather Chemists Association. 103(9):290-297.
- Cardamone, J.M., Nunez, A., Garcia, R.A., Ramos, M. 2009. Characterizing Wool Keratin. Research Letters in Materials Science. 2009(5). Available: http://www.hindawi.com/journals/rlms/2009/147175.abs.html.
- Brown, E.M. 2009. Collagen a natural scaffold for biology and engineering. Journal of American Leather Chemists Association. 104(8):275-285.
- Cardamone, J.M. 2007. Enzyme-mediated crosslinking of wool part I: transglutaminase. Textile Research Journal. 77(4):214-221.
- Cardamone, J.M., Phillips, J.G. 2007. Enzyme-mediated Crosslinking of Wool Part II: Keratin and Transglutaminase. Textile Research Journal. 77(5):277- 283.
- Cardamone, J.M. Keratin Transamidation. 2008. International Journal of Biological Macromolecules. 42(5):413-419.
- Taylor, M.M., Marmer, W.N., Brown, E.M. 2008. Effect of Fillers Prepared from Enzymatically Modified Proteins on Mechanical Properties of Leather. Journal of American Leather Chemists Association. 103(4):128-137.
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Progress 10/01/06 to 09/30/07
Outputs
Progress Report Objectives (from AD-416) 1. Functional modification, leather and leather byproducts: Develop a foundation for the use of new chemical and biochemical technologies (a) in the production of high quality chrome-free leathers, (b) in expanding the range of high value biomaterial applications for solubilized proteins from leather byproducts. 2. Functional modification, wool: Modify wool to impart functionality for improved performance and expanded uses of domestic wool. Approach (from AD-416) 1. Collagen modification is central to both tanning and byproduct utilization. (a) To develop a basis for designing or selecting effective sustainable tanning agents, the results of theoretical and experimental model studies will be integrated to give the best overall evaluation. Targets for chrome-free tanning agents will include natural products (tannins, genipin), enzymes for protein modification (transglutaminase, oxidases), and organic chemicals (aldehydes, acrylates). (b) Gelatin byproducts from leather processing will be evaluated alone and in combination with other proteins from renewable agricultural resources as potential coatings and fillers for use in leather or wool processing. Partially hydrolyzed collagen recovered from leather waste will also be combined with fibrous protein waste products for the preparation of novel composite materials with useful properties, such as high strength and thermal stability, for use in a variety of industrial applications, such as "bonded" leather and shoe inner soles. 2. The ERRC process (patent pending) of treating wool fabric for shrinkage control will be evaluated on wool blended with other natural and synthetic fibers, and yarn-dyed fabrics. Chemical and biochemical modifications of intact wool to add functionality will be evaluated for improved properties, such as softness, comfort, resistance to shrinkage, improved flame retardancy, and resistance to photodegradation. Collagen hydrolysates, or other proteinaceous carriers, will be applied to wool fabric as a vehicle for introducing agents that impart such properties as improved whiteness, resistance to ignition, and photoprotection. Significant Activities that Support Special Target Populations This report serves to document research conducted under Trust Fund Cooperative Agreement #58-1935-1-143 (1935-41440-014-01T) between ARS and the American Sheep Industry Association (ASI). Although the consumer recognizes wool for its unique properties of resiliency and warmth, its apparent discomfort and lack of dimensional stability limit apparel production and consumer acceptance. Foreign imports of wool treated by chlorination (not permitted in the USA) threaten markets for domestic wool. Earlier ARS research under 1935-41440-011-01T resulted in an aqueous enzymatic process that whitens, biopolishes, and prevents wool from shrinking. Mill trials have been conducted at three dye and finishing plants with ASI representative and ARS scientist providing technical assistance to apply the ARS process to more than 700 yards of wool fabric from textile converters that produce fabrics for commercial products. These yardages were ARS-processed to fill military contracts for undergarments that are in the final stages of wear-testing in the field. This report serves to document research conducted under USDA Specific Cooperative Agreement # 58-1935-4-0442 (1935-41440-014-02S) with the Univ. of Georgia, to facilitate the work underwritten by base funds and TFCA - 014-01T (above) between ARS and ASI. To fully meet the flame retardant requirements for military attire, wool fiber is currently blended with Nomex or Kevlar. To improve the flame retardant properties of ARS- processed wool, temperature-resistant, high-performance polymers, polyimidesiloxanes, were synthesized and applied to wool fabric. The burning resistance of the treated fabric equals that of a wool/Nomex fabric blend intended for military attire. Notice of allowance was granted (3/09/07) for patent application US 2006/0075574. A confidentiality agreement for further development of the technology to determine feasibility of commercialization was signed on 5/10/07. This report serves to document research conducted under Non-Funded Cooperative Agreement #58-1935-6-0615N (1935-41440-03N) between ARS and Philadelphia Univ. As MS degree thesis research, a student was to examine the effect of the application of commercial flame retardant chemicals onto fabric that had been mill-processed with the ARS treatment for military underwear to provide a basis of comparison for flame retardant tests on ARS-processed wool treated with the polyimidesiloxanes developed under SCA -014-02S (cf above). PI notified ARS that the student left campus without completing the research. This report serves to document research conducted under Non-Funded Cooperative Agreement #58-1935-6-648N (1935-41440-014-04N) between ARS and Elementis LTP, LP. The objective of this cooperative agreement is to characterize and evaluate a novel-tanning chemical. In the first phase a new Elementis product would be characterized and, in the second phase, the product would be evaluated in pilot scale trials for application to limed and bated hides. The chemical was received and analyzed, and the results were communicated by email to the industrial partner to complete the first phase. The partner chose not to pursue the second phase. Accomplishments Enzymatic stabilization of wool: Shrinkproofing wool to control felting and dimensional stability by the ARS process utilizing oxidation and enzyme treatment can result in up to 18% fabric strength loss. When a common crosslinking enzyme, transglutaminase, was applied to ARS- processed wool fabrics, up to 5% strength was regained. The chemical properties of wool that make it dyeable and available to other chemical finishing processes were not affected. These results lay the groundwork for other chemical changes in wool designed not only to improve physical properties but also to produce novel value-added wool products. (NP 306, Quality and Utilization of Agricultural Products; Component 2. New Processes, New Uses, and Value-Added Foods and Biobased Products; Problem Area 2c. New and Improved Processes and Feedstocks) Biobased fillers for leather: To make a uniform product, tanners typically fill the hide with petroleum-derived materials. In response to increasing demand for biobased products, we demonstrated that gelatin (a byproduct of leather production) when enzymatically crosslinked with casein or whey (byproducts of the dairy industry) produced biopolymers with unique properties. These mixed polymerized proteins when applied to partially processed hides, were evenly distributed throughout the hide and, more importantly, were not removed by washing. Thus, we have added value to waste products from various agricultural sources by making products that have potential use in the leather-making process. (NP 306, Quality and Utilization of Agricultural Products; Component 2. New Processes, New Uses, and Value-Added Foods and Biobased Products; Problem Area 2b. New Uses for Agricultural By-products) Understanding tanning at the molecular level: The staggering of triple helical collagen monomers in the assembly of the fibril results in overlap bands with dense lateral packing and gap domains of low-density molecular packing. Most studies of artificially stabilized collagen focus on crosslinks that utilize specific amino acid side chains, without considering whether these are more likely to be located in overlap or gap regions. The gap region with its lower molecular density appears promising as an area able to accommodate oligomeric compounds that are the typical tanning agents. This study uses the ERRC collagen microfibril model to explore the potential effects on the secondary and tertiary structure of collagen when tanning agents of different types are stabilized within the gap region of the microfibril. The method will be valuable in predicting the effectiveness of proposed new tanning agents. (NP 306, Quality and Utilization of Agricultural Products; Component1. Quality Characterization, Preservation, and Enhancement; Problem Area 1a. Definition and Basis for Quality) Technology Transfer Number of U.S. Patents granted: 2 Number of new Commercial Licenses granted: 1 Number of Non-Peer Reviewed Presentations and Proceedings: 7 Number of Newspaper Articles,Presentations for NonScience Audiences: 1
Impacts
(N/A)
Publications
- Brown, E.M., Stauffer, D.M., Cooke, P.H., Maffia, G.J. 2006. The effect of ultrasound on bovine hide collagen structure. Journal of American Leather Chemists Association. 101(7):274-283.
- Ding, K., Taylor, M.M., Brown, E.M. 2006. Effect of Genipin on the Thermal Stability of Hide Powder. Journal of American Leather Chemists Association. 101(10):362-367.
- Kolomaznik, K., Bailey, D.G., Taylor, M.M. 2007. Deliming of un-bounded and bounded lime from white hide. Journal of American Leather Chemists Association. 102(5):158-163.
- Taylor, M.M., Marmer, W.N., Brown, E.M. 2007. Evaluation of Polymers Prepared from Gelatin and Casein or Whey as Potential Fillers. Journal of American Leather Chemists Association. 102(4):111-120.
- Ding, K., Taylor, M.M., Brown, E.M. 2007. Genipin -Aluminum or -Vegetable Tannin Combinations on Hide Powder. Journal of American Leather Chemists Association. 102(5):164-170.
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Progress 10/01/05 to 09/30/06
Outputs
Progress Report 1. What major problem or issue is being resolved and how are you resolving it (summarize project aims and objectives)? How serious is the problem? Why does it matter? This project addresses utilization of the major byproducts--hides and wool--of cattle and sheep, animals raised domestically for their meat. The research contributes directly to National Program #306, "Quality, and Utilization of Agricultural Products," and particularly to its component on New Processes, New Uses, and Value-added Foods and Biobased Products. It addresses the following goals: * New knowledge derived from improved understanding of the structure, properties, and function of animal components, particularly proteins will generate development of a variety of new industrial products. * New technologies to convert commodities and process byproducts into important value-added products such as improved textiles will fill demonstrated needs. (a) Functional modification, leather and
leather byproducts: Animal hides are high value coproducts of the meat industry, and the U.S. beef industry is the major, worldwide, source of cattle hides, valued at over $1 billion annually, for leather production. Tanning, the process of converting hides into high value, durable leather is rapidly being transferred to countries with lower environmental standards and labor costs. The result has been a major loss of jobs in the domestic leather industry, which is partially offset by the opening of tanneries associated with meat packing facilities where some chrome tanning of hides into unfinished leather ("wet blue") is now occurring. The processes used to convert two tons of "wet blue" into finished automotive upholstery leather leave the processor with a ton of solid waste, mainly a complex of collagen with chromium. We have developed a cost effective process for converting this waste, currently deposited in landfills, into high-grade technical gelatin, and collagen
hydrolysate. Lack of domestic markets for this technical gelatin has hindered the adoption of this process by the U.S. leather industry. Development of high quality chrome- free leathers in response to the preferences of consumers, particularly in European markets, is hindered by a lack of understanding of tanning mechanisms. (b) Functional modification, wool: The U.S. sheep industry, a smaller but important component of the meat industry, produces 40 million pounds of raw wool per year. Domestic wool is threatened by the influx of imported wool treated for shrinkage resistance by chlorination, a process that produces large amounts of absorbable organo-halogens (AOX). Although some U.S. wool is exported for processing, the military and many law enforcement agencies are required to use domestically raised and processed wool for their uniforms and other products. Representatives of the armed forces have expressed interest in replacing synthetic materials in undergarments with
comfortable wool. They are currently evaluating wool modified by an enzymatic process developed at ERRC in the predecessor project. Meeting additional needs of the military for altered wool propertiesnon-flame- ignitability, navy whiteness, and oil and water repellencyrequires further research on the functional modification of this woolen fabric. Domestic wool has properties that limit its acceptance and competitiveness when compared to imported wool. Environmentally benign methods for adding value to U.S. wool will encourage domestic processing while reducing the reliance on imports. 2. List by year the currently approved milestones (indicators of research progress) FY2005: 15 months (6/30/04 - 9/30/05) Objective 1 Functional modification, leather and leather byproducts: Develop a foundation for the use of new chemical and biochemical technologies (a) in the production of high quality chrome-free leathers, (b) in expanding the range of high value biomaterial applications for
solubilized proteins from leather byproducts. Objective 1a: High quality chrome-free leather. Develop a foundation for the use of new chemical and biochemical technologies (a) in the production of high quality chrome-free leathers, and pursue the development of a general mechanism for tanning. 1a. Computational: Initiate the theoretical evaluation of the effects of collagen modifications, via tanning chemicals or natural aging, on the conformational stability of collagen microfibrils and the ultimate thermal stability of the collagen matrix. Experimental: Initiate evaluation of the effects of chemical or physical modifications to collagen, as an isolated protein or in the hide matrix, on its interactions with potential tanning complexes. Objective 1b. Functional modification, leather and leather byproducts: Develop a foundation for the use of new chemical and biochemical technologies (b) in expanding the range of high value biomaterial applications for solubilized proteins from
leather byproducts, especially where these applications are in the manufacturing of leather. 1b. Solubilized proteins from leather byproducts: Identify chemoenzymatic modification strategies for processing proteinaceous byproducts of leather manufacturing to form biopolymers or conjugates with other surplus agricultural proteins. Initiate the chemical and physical evaluation of these products and their potential for utilization in leather manufacturing processes. Objective 2: Functional modification, wool: Modify wool to impart functionality for improved performance and expanded uses of domestic wool in nontraditional markets. 2. Initiate mill trials to establish optimized conditions for making "biopolished" (surface-oxidized and enzymatically polished) wool, developed and patented under the predecessor project, for minimizing shrinkage of woven or knit wool and its blends with other fibers and for improving the "handle" or feel of those textiles. FY2006: 27 months (9/30/05 -
9/30/06) 1a. Computational: Continue the evaluation of the effects of modifications to collagen on the conformation and conformational stability of collagen microfibrils. Experimental: Continue the evaluation of the effects of modifications to collagen, as an isolated protein or in the hide matrix, on its interactions with potential tanning complexes. Initiate the experimental evaluation of computationally favorable modifications. 1b. Apply chemoenzymatic modification strategies identified in the previous year, for processing proteinaceous byproducts of leather manufacturing to produce biopolymers or conjugates in sufficient quantity for evaluation of chemical and physical properties. Continue the chemical and physical evaluation of these products and their potential for utilization in leather manufacturing processes. 2. Modify the patented wool process as needed, based on the results of mill trials. Initiate the development of environmentally acceptable methods for functionalizing
wool for improved performance characteristics. FY2007 39 months (9/30/06- 9/30/07): 1a. Computational: Continue the evaluation of the effects of collagen modifications on the conformation and conformational stability of collagen microfibrils. Initiate the theoretical evaluation of the interactions of potential enzymatic or other chromium-free tanning reagents with microfibrillar collagen. Experimental: Continue the evaluation of the effects of computationally favorable modifications to collagen, as an isolated protein or in the hide matrix, on its interactions with potential tanning complexes. 1b. Continue the evaluation of chemical, physical and functional properties of those products that show promise for applications in leather manufacturing. Initiate pilot scale application of identified products to pieces of hide or partially processed leather. Initiate the quality evaluation of leather manufactured with the identified products. 2. Select the most promising functionalized
substrates as starting products for the engineering of new as well as improved conventional textile products. Initiate the optimization of processes for improving selected functionality. FY2008: 51 months (9/30/07 - 9/30/08) 1a. Computational: Complete the evaluation of the effects of collagen modifications on the conformation and conformational stability of collagen microfibrils. Continue the estimation of the potential for enzymatic or other chromium-free tannages. Experimental: See previous periods. Transfer methods developed on isolated collagen to hide powder or intact hide. 1b. Continue the evaluation of leather produced at the pilot scale using the identified products. Identify an industrial partner for full scale testing of the identified products in leather manufacturing. Initiate full-scale tests of the use of feasible products in leather manufacturing. 2. Initiate pilot scale processing and evaluation of functionalized textile products using substrates identified in
previous year. Initiate cost analysis of technically feasible processes. FY2009: 60 months (9/30/08 - 6/30/09) 1a. Computational: Complete the theoretical evaluation of the potential for enzymatic or other chromium-free tannages. Contribute concepts developed in previous periods to the development of a fundamental understanding of tanning. Experimental: Continue transfer of methods from collagen to intact hide. Formulate a set of options based on technical and economic factors for selecting or designing a high quality chrome-free tannage. 1b. Continue full-scale tests of promising processes. Perform cost analysis for promising processes. Initiate transfer of technology to industry. 2. Complete cost analysis for technically feasible processes. Document performance aspects of products and modify functionality and/or textile substrate to optimize identified end-uses. Transfer technology to industry as appropriate. 4a List the single most significant research accomplishment during
FY 2006. Genipin as a potential tanning agent: Tanning of animal hides or skins produces leather, a high value co-product of the meat industry. Salts of the mineral chromium are the most commonly used tanning agents for the production of high quality leathers. Because of environmental considerations, and customer preference, the tanning industry is interested in developing chrome-free tannages. Although the art of tanning is highly developed, the mechanisms are poorly understood. The research reported here is a first step in the evaluation of genipin, a small molecule isolated from the fruit of the gardenia plant, as a potential tanning agent. The tanning effect of genipin was found to be similar to that of glutaraldehyde, an organic tanning agent currently being used to produce chrome-free leather. A major advantage of genipin over glutaraldehyde is a much lower level of toxicity. The development of genipin as a tanning agent could provide the leather industry with a
biofriendly, safe formulation for production of high quality chrome-free leathers. This accomplishment contributes directly to National Program #306, Component 2, Objective 1a. 4d Progress report. 1935-41440-014-01T-This report serves to document research conducted under Trust Fund Cooperative Agreement between ARS and the American Sheep Industry Association (ASI). Although the consumer recognizes wool for its unique properties of resiliency and warmth, its apparent discomfort and lack of dimensional stability limit apparel production and consumer acceptance. Foreign imports of wool treated by chlorination (not permitted in the United States) threaten markets for domestic wool. ARS Research under the previous project 1935-41440-011-01T resulted in an aqueous enzymatic process that whitens, biopolishes, and prevents wool from shrinking. The American Sheep Industry Association (ASI), the military, and the domestic wool industry now indicate particular attention should be given to
flame retardation or prevention to meet the needs of the military. Wool will ignite and burn with a self-extinguishing flame. To meet the needs of the military for itch-free, machine washable wool with improved burn-prevention behavior, CWU researchers have developed a heat-resistant polymer to apply to ARS-processed wool fabric. The burning resistance of the treated fabric equals that of a wool/ Nomex fabric blend intended for military attire. The ARS product is preferred because it produces a soft crushable ash whereas the blend produces an intractable residue that can lodge in open wounds. ARS is introducing the military to comfortable, machine washable wool fabrics with improved flame retardancy (FR). This product will increase the demand for domestic wool fabrics that are processed entirely by textile mills in this country. This research concerns the apparel needs of the military in wartime and the textile industry recognizes that these developments will create novel
commercial markets for wool. 1935-41440-014-02S-This report serves to document research conducted under a Specific Cooperative Agreement between ARS and the University of Georgia, which facilitated the work underwritten by base funds and Trust Fund Cooperative Agreement #58-1935-1-143 between ARS and the American Sheep Industry Association (ASI); see report for 1935-41440-014-01T). Wool fibers are flammable but the propagating flame self-extinguishes and produces a soft ash residue unlike the melt-drip behavior of synthetic fibers that form a molten, hard bead upon cooling. Because of its self- extinguishing property, wool is used in airplane interiors and ARS- processed wool fabrics that overcome the "itch-factor" are preferred by the military to replace synthetic polypropylene underwear. To fully meet the flame retardant requirements for military attire, wool fiber is currently blended with Nomex or Kevlar (synthetic fibers known to resist burning). To improve the flame retardant
properties of ARS-processed wool, a temperature-resistant, high-performance polymer that can be applied to wool fabric was synthesized. The burning resistance of the treated fabric equals that of a wool/ Nomex fabric blend intended for military attire. The polymer incorporates the highly ordered structure of polyimide with soft segments of siloxanes to form nonignitable polyimidesiloxanes that are easy to process and exhibit thermal and radiation stability, stain and water resistance, and stability to UV light. Successful completion of this research will introduce the military to comfortable, machine-washable wool fabrics that will resist burning. To meet the military demand for these fabrics, participating wool mills are anticipated to include ERRC technology in their existing product lines, thereby increasing the demand for domestic wool fiber and apparel for traditional and new end uses. 1935-41440-014-03N-This report serves to document research conducted under a Specific
Cooperative Agreement between ARS and the Philadelphia University. Research on flame-retardant wool was continued under this new agreement. As thesis research for a Master's degree, a student at Philadelphia University is examining the effect of the application of commercial flame retardant chemicals onto ARS-processed wool (fabric that had been mill-processed with the ARS treatment for military underwear). He is applying commercial fire retardant agents to untreated wool to serve as a basis for comparison to polyimidesiloxane applications to untreated and ARS-processed wool of the same type fabric. Some fabrics included in the study are ARS-processed and dyed military green from mill trials undertaken to fill military contracts for machine-washable wool. His work will provide the basis of comparison for flame retardant tests on ARS-processed wool treated with the polyimidesiloxanes developed under 1935-41440-014-02S (described above). 5. Describe the major accomplishments to date
and their predicted or actual impact. Major accomplishment from FY-2005: Leather byproduct utilization: CWU researchers demonstrated that biopolymers can be produced by enzymatically crosslinking gelatin, recovered from cattle hides as a byproduct of tanning, with other surplus agricultural proteins. Sodium caseinate and ovalbumin, both proteins historically used in leather processing, were individually combined with gelatin and then treated with enzyme to form conjugates that had unique physical properties. Sodium caseinate is highly soluble and reactive under conditions favorable for enzymatic crosslinking with gelatin to form high molecular weight complexes. High viscosity biopolymers are formed by enzymatic crosslinking of ovalbumin, which is less soluble than sodium caseinate and forms colloidal suspensions, with gelatin. The degree of crosslinking was enhanced by addition of even small amounts of the secondary protein. Economically, the current costs of sodium caseinate
($1.95/lb) and ovalbumin ($1.80/lb), while not insignificant, are less than that of lowest grade gelatin ($2.60-2.75/lb). These protein conjugates are anticipated to replace petroleum-derived resins in leather fillers and finishing agents. (NP306, Component II; Milestone: Objective 1a) 6. What science and/or technologies have been transferred and to whom? When is the science and/or technology likely to become available to the end- user (industry, farmer, other scientists)? What are the constraints, if known, to the adoption and durability of the technology products? Functional modification of collagen: - The collagen microfibril molecular model developed under previous projects is now providing a basis for research into the interactions of collagen with tannin-like molecules, and the effects of changes in ionic strength and pH on collagen by researchers in Europe. The model has recently been acquired by medical researchers in the USA and China. Functional modification of leather
byproducts: - Continued MOU with Dr. Karel Kolomaznik, Professor, Tomas Bata University, Zlin, Czech Republic, in which the protein hydrolysate from waste leather products will be used to lower the formaldehyde content in resins. - Continued MOU with Dr. Jaume Cot, Professor, Departamento de Ecotecnologias, CSIC, Barcelona, Spain, for research on enzymatic modification of collagen by-products. Functional modification of wool: - Mill trials of the now patented process developed under Trust Fund Agreement 58-1935-1-143 with the American Sheep Industry Association (ASI) are being conducted under more than 20 individual confidentiality agreements with American wool mills. More than 20,000 pounds of wool fabric have been ARS-processed in finishing and dyeing plants throughout the country with plans to treat to treat raw wool fiber and wool yarns for commercial and handcrafter markets. One particular mill has applied the process continuously over the past year and is now petitioning to
license with the intention to supply the military with itch-free, machine- washable wool for underwear. They are supplying the military with 10,000 ARS-processed undershirts for the first and second stages of wear trials by troops in the field. They plan to use the technology for private- sector products, for which the license is required. - ARS has published its intent to license the ARS process, and is currently reviewing several applications for such licensing. 7. List your most important publications in the popular press and presentations to organizations and articles written about your work. (NOTE: List your peer reviewed publications below). Reports on the hides and leather phases of this project were presented to customers at the annual meeting of the Research Liaison Committee of the American Leather Chemists Association, ERRC, Wyndmoor, PA, April 25-26, 2006 (industry, academic, government representatives of the hides, leather, and tannery supplier industries). Progress
reports on collaborative wool research with the American Sheep Industry Association (ASI) were prepared monthly for ASI review and presented in quarterly meetings at ERRC to an ASI representative.
Impacts
(N/A)
Publications
- Ding, K., Taylor, M.M., Brown, E.M. 2006. Tanning potential of genipin [abstract]. American Leather Chemists Association Meeting. Paper No. 17.
- Cardamone, J.M., Yao, J. 2005. Activated peroxide-assisted enzymatic control of wool shrinkage [abstract]. 11th International Wool Research Conference. p. 36CCF.
- Cardamone, J.M. 2005. Novel chemoenzymatic system for effective wool bleaching, biopolishing, and shrinkage control. Program No. 432 [CD-ROM]. 2005 Abstract Viewer. Honolulu, Hawaii: International Chemical Congress of Pacific Basin Societies.
- Cardamone, J.M., Kanchagar, A.P. 2005. Method of inhibiting the burning of natural fibers, synthetic fibers, or mixtures thereof, or fabric or yarn composed of natural fibers, synthetic fibers, or mixtures thereof, and products produced by such methods. Patent Application. Ser. No. 11/211,828.
- Chen, T., Embree, H.D., Brown, E.M., Taylor, M.M., Payne, G.F. 2006. Polysaccharide-based polymers and methods of making the same. Patent Application. Ser. No. 10/529,012. US Patent 7,138,373 issued November 21, 2006.
- Taylor, M.M., Bumanlag, L.P., Marmer, W.N., Brown, E.M. 2006. Use of enzymatically modified gelatin and casein as fillers in leather processing. Journal of American Leather Chemists Association. 101(5):169-178.
- Taylor, M.M., Marmer, W.N., Brown, E.M. 2006. Preparation and characterization of biopolymers derived from enzymatically modified gelatin and whey. Journal of American Leather Chemists Association. 101(6) :235-248.
- Brown, E.M., Dudley, R.L. 2005. Approach to a tanning mechanism: study of the interaction of aluminum sulfate with collagen. Journal of American Leather Chemists Association. 100(10):401-409.
- Cardamone, J.M., Damert, W.C. 2006. Low temperature dyeing of wool processed for shrinkage control. Textile Research Journal. 76(1):78-85.
- Cardamone, J.M., Nunez, A., Ashby, R.D., Dudley, R.L. 2006. Activated peroxide for enzymatic control of wool shrinkage part 1: elucidation. Textile Research Journal. 76(2):99-108.
- Cardamone, J.M. 2006. Activated peroxide for enzymatic control of wool shrinkage part ii: wool and other fiber-type fabrics. Textile Research Journal. 76(2):109-115.
- Taylor, M.M., Marmer, W.N., Brown, E.M. 2006. Effect of fillers prepared from enzymatically modified proteins on mechanical properties of leather [abstract]. American Leather Chemists Association Meeting. Paper No. 3.
- Kolomaznik, K., Bailey, D.G., Taylor, M.M. 2006. Deliming of bound and un- bound lime from white hide [abstract]. American Leather Chemists Association Meeting. Paper No. 13.
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Progress 10/01/04 to 09/30/05
Outputs
1. What major problem or issue is being resolved and how are you resolving it (summarize project aims and objectives)? How serious is the problem? What does it matter? This project addresses utilization of the major byproducts--hides and wool--of cattle and sheep, animals raised domestically for their meat. The research contributes directly to National Program #306, "Quality, and Utilization of Agricultural Products," and particularly to its component on New Processes, New Uses, and Value-added Foods and Biobased Products. It addresses the following goals: * New knowledge derived from improved understanding of the structure, properties, and function of animal components, particularly proteins will generate development of a variety of new industrial products. * New technologies to convert commodities and process byproducts into important value-added products such as improved textiles will fill demonstrated needs. (a) Functional modification, leather and leather
byproducts: Animal hides are high value coproducts of the meat industry, and the U.S. beef industry is the major, worldwide, source of cattle hides, valued at over $1 billion annually, for leather production. Tanning, the process of converting hides into high value, durable leather is rapidly being transferred to countries with lower environmental standards and labor costs. The result has been a major loss of jobs in the domestic leather industry, which is partially offset by the opening of tanneries associated with meat packing facilities where some chrome tanning of hides into unfinished leather ("wet blue") is now occurring. The processes used to convert two tons of "wet blue" into finished automotive upholstery leather leave the processor with a ton of solid waste, mainly a complex of collagen with chromium. We have developed a cost effective process for converting this waste, currently deposited in landfills, into high-grade technical gelatin, and collagen hydrolysate. Lack
of domestic markets for this technical gelatin has hindered the adoption of this process by the U.S. leather industry. Development of high quality chrome- free leathers in response to the preferences of consumers, particularly in European markets, is hindered by a lack of understanding of tanning mechanisms. (b) Functional modification, wool: The U.S. sheep industry, a smaller but important component of the meat industry, produces 40 million pounds of raw wool per year. Domestic wool is threatened by the influx of imported wool treated for shrinkage resistance by chlorination, a process that produces large amounts of absorbable organo-halogens (AOX). Although some U.S. wool is exported for processing, the military and many law enforcement agencies are required to use domestically raised and processed wool for their uniforms and other products. Representatives of the armed forces have expressed interest in replacing synthetic materials in undergarments with comfortable wool. They
are currently evaluating wool modified by an enzymatic process developed at ERRC in the predecessor project. Meeting additional needs of the military for altered wool propertiesnon-flame- ignitability, navy whiteness, and oil and water repellencyrequires further research on the functional modification of this woolen fabric. Domestic wool has properties that limit its acceptance and competitiveness when compared to imported wool. Environmentally benign methods for adding value to U.S. wool will encourage domestic processing while reducing the reliance on imports. 2. List the milestones (indicators of progress) from your Project Plan. FY2005: 15 months (6/30/04 - 9/30/05) Objective 1 Functional modification, leather and leather byproducts: Develop a foundation for the use of new chemical and biochemical technologies (a) in the production of high quality chrome-free leathers, (b) in expanding the range of high value biomaterial applications for solubilized proteins from leather
byproducts. Objective 1a: High quality chrome-free leather. Develop a foundation for the use of new chemical and biochemical technologies (a) in the production of high quality chrome-free leathers, and pursue the development of a general mechanism for tanning. 1a. Computational: Initiate the theoretical evaluation of the effects of collagen modifications, via tanning chemicals or natural aging, on the conformational stability of collagen microfibrils and the ultimate thermal stability of the collagen matrix. Experimental: Initiate evaluation of the effects of chemical or physical modifications to collagen, as an isolated protein or in the hide matrix, on its interactions with potential tanning complexes. Objective 1b. Functional modification, leather and leather byproducts: Develop a foundation for the use of new chemical and biochemical technologies (b) in expanding the range of high value biomaterial applications for solubilized proteins from leather byproducts, especially where
these applications are in the manufacturing of leather. 1b. Solubilized proteins from leather byproducts: Identify chemoenzymatic modification strategies for processing proteinaceous byproducts of leather manufacturing to form biopolymers or conjugates with other surplus agricultural proteins. Initiate the chemical and physical evaluation of these products and their potential for utilization in leather manufacturing processes. Objective 2: Functional modification, wool: Modify wool to impart functionality for improved performance and expanded uses of domestic wool in nontraditional markets. 2. Initiate mill trials to establish optimized conditions for making biopolished (surface-oxidized and enzymatically polished) wool, developed and patented under the predecessor project, for minimizing shrinkage of woven or knit wool and its blends with other fibers and for improving the handle or feel of those textiles. FY2006: 27 months (9/30/05 - 9/30/06) 1a. Computational: Continue the
evaluation of the effects of modifications to collagen on the conformation and conformational stability of collagen microfibrils. Experimental: Continue the evaluation of the effects of modifications to collagen, as an isolated protein or in the hide matrix, on its interactions with potential tanning complexes. Initiate the experimental evaluation of computationally favorable modifications. 1b. Apply chemoenzymatic modification strategies identified in the previous year, for processing proteinaceous byproducts of leather manufacturing to produce biopolymers or conjugates in sufficient quantity for evaluation of chemical and physical properties. Continue the chemical and physical evaluation of these products and their potential for utilization in leather manufacturing processes. 2. Modify the patented wool process as needed, based on the results of mill trials. Initiate the development of environmentally acceptable methods for functionalizing wool for improved performance
characteristics. FY2007 39 months (9/30/06- 9/30/07): 1a. Computational: Continue the evaluation of the effects of collagen modifications on the conformation and conformational stability of collagen microfibrils. Initiate the theoretical evaluation of the interactions of potential enzymatic or other chromium-free tanning reagents with microfibrillar collagen. Experimental: Continue the evaluation of the effects of computationally favorable modifications to collagen, as an isolated protein or in the hide matrix, on its interactions with potential tanning complexes. 1b. Continue the evaluation of chemical, physical and functional properties of those products that show promise for applications in leather manufacturing. Initiate pilot scale application of identified products to pieces of hide or partially processed leather. Initiate the quality evaluation of leather manufactured with the identified products. 2. Select the most promising functionalized substrates as starting products
for the engineering of new as well as improved conventional textile products. Initiate the optimization of processes for improving selected functionality. FY2008: 51 months (9/30/07 - 9/30/08) 1a. Computational: Complete the evaluation of the effects of collagen modifications on the conformation and conformational stability of collagen microfibrils. Continue the estimation of the potential for enzymatic or other chromium-free tannages. Experimental: See previous periods. Transfer methods developed on isolated collagen to hide powder or intact hide. 1b. Continue the evaluation of leather produced at the pilot scale using the identified products. Identify an industrial partner for full scale testing of the identified products in leather manufacturing. Initiate full-scale tests of the use of feasible products in leather manufacturing. 2. Initiate pilot scale processing and evaluation of functionalized textile products using substrates identified in previous year. Initiate cost
analysis of technically feasible processes. FY2009: 60 months (9/30/08 - 6/30/09) 1a. Computational: Complete the theoretical evaluation of the potential for enzymatic or other chromium-free tannages. Contribute concepts developed in previous periods to the development of a fundamental understanding of tanning. Experimental: Continue transfer of methods from collagen to intact hide. Formulate a set of options based on technical and economic factors for selecting or designing a high quality chrome-free tannage. 1b. Continue full-scale tests of promising processes. Perform cost analysis for promising processes. Initiate transfer of technology to industry. 2. Complete cost analysis for technically feasible processes. Document performance aspects of products and modify functionality and/or textile substrate to optimize identified end-uses. Transfer technology to industry as appropriate. 3a List the milestones that were scheduled to be addressed in FY 2005. For each milestone,
indicate the status: fully met, substantially met, or not met. If not met, why. 1. Computational: Initiate the theoretical evaluation of the effects of collagen modifications, via tanning chemicals or natural aging, on the conformational stability of collagen microfibrils and the ultimate thermal stability of the collagen matrix. Milestone Fully Met 2. Experimental: Initiate evaluation of the effects of chemical or physical modifications to collagen, as an isolated protein or in the hide matrix, on its interactions with potential tanning complexes. Milestone Fully Met 3. Identify chemoenzymatic modification strategies for processing proteinaceous byproducts of leather manufacturing to form biopolymers or conjugates with other surplus agricultural proteins. Milestone Fully Met 4. Initiate the chemical and physical evaluation of these products and their potential for utilization in leather manufacturing processes. Milestone Fully Met 5. Initiate mill trials to establish optimized
conditions for making "biopolished" (surface-oxidized and enzymatically polished) wool, developed and patented under the predecessor project, for minimizing shrinkage of woven or knit wool and its blends with other fibers and for improving the "handle" or feel of those textiles. Milestone Fully Met 3b List the milestones that you expect to address over the next 3 years (FY 2006, 2007, and 2008). What do you expect to accomplish, year by year, over the next 3 years under each milestone? FY2006: 27 months (9/30/05 - 9/30/06) 1a. Computational: Continue the evaluation of the effects of modifications to collagen on the conformation and conformational stability of collagen microfibrils. Experimental: Continue the evaluation of the effects of modifications to collagen, as an isolated protein or in the hide matrix, on its interactions with potential tanning complexes. Initiate the experimental evaluation of computationally favorable modifications. 1b. Apply chemoenzymatic modification
strategies, identified in the previous year, for processing proteinaceous byproducts of leather manufacturing to produce biopolymers or conjugates in sufficient quantity for evaluation of chemical and physical properties. Continue the chemical and physical evaluation of these products and their potential for utilization in leather manufacturing processes. 2. Modify the patented wool process as needed, based on the results of mill trials. Initiate the development of environmentally acceptable methods for functionalizing wool for improved performance characteristics. FY2007 39 months (9/30/06- 9/30/07): 1a. Computational: Continue the evaluation of the effects of collagen modifications on the conformation and conformational stability of collagen microfibrils. Initiate the theoretical evaluation of the interactions of potential enzymatic or other chromium-free tanning reagents with microfibrillar collagen. Experimental: Continue the evaluation of the effects of computationally
favorable modifications to collagen, as an isolated protein or in the hide matrix, on its interactions with potential tanning complexes. 1b. Continue the evaluation of chemical, physical and functional properties of those products that show promise for applications in leather manufacturing. Initiate pilot scale application of identified products to pieces of hide or partially processed leather. Initiate the quality evaluation of leather manufactured with the identified products. 2. Select the most promising functionalized substrates as starting products for the engineering of new as well as improved conventional textile products. Initiate the optimization of processes for improving selected functionality. FY2008: 51 months (9/30/07 - 9/30/08) 1a. Computational: Complete the evaluation of the effects of collagen modifications on the conformation and conformational stability of collagen microfibrils. Continue the estimation of the potential for enzymatic or other chromium-free
tannages. Experimental: See previous periods. Transfer methods developed on isolated collagen to hide powder or intact hide. 1b. Continue the evaluation of leather produced at the pilot scale using the identified products. Identify an industrial partner for full scale testing of the identified products in leather manufacturing. Initiate full-scale tests of the use of feasible products in leather manufacturing. 2. Initiate pilot scale processing and evaluation of functionalized textile products using substrates identified in previous year. Initiate cost analysis of technically feasible processes. 4a What was the single most significant accomplishment this past year? Leather byproduct utilization: CWU researchers demonstrated that biopolymers can be produced by enzymatically crosslinking gelatin, recovered from cattle hides as a byproduct of tanning, with other surplus agricultural proteins. Sodium caseinate and ovalbumin, both proteins historically used in leather processing,
were individually combined with gelatin and then treated with enzyme to form conjugates that had unique physical properties. Sodium caseinate is highly soluble and reactive under conditions favorable for enzymatic crosslinking with gelatin to form high molecular weight complexes. High viscosity biopolymers are formed by enzymatic crosslinking of ovalbumin, which is less soluble than sodium caseinate and forms colloidal suspensions, with gelatin. The degree of crosslinking was enhanced by addition of even small amounts of the secondary protein. Economically, the current costs of sodium caseinate ($1.95/lb) and ovalbumin ($1.80/lb), while not insignificant, are less than that of lowest grade gelatin ($2.60-2.75/lb). These protein conjugates are anticipated to replace petroleum derived resins in leather fillers and finishing agents. (NP306, Component II; Milestone: Objective 1a) 4d Progress report. 1935-41440-014-01T-This report serves to document research conducted under Trust Fund
Cooperative Agreement between ARS and the American Sheep Industry Association (ASI). Although the consumer recognizes wool for its unique properties of resiliency and warmth, its apparent discomfort and lack of dimensional stability limit apparel production and consumer acceptance. Foreign imports of wool treated by chlorination (not permitted in the United States) threaten markets for domestic wool. ARS Research under the previous project 1935-41440-011-01T resulted in an aqueous enzymatic process that whitens, biopolishes, and prevents wool from shrinking. The American Sheep Industry Association (ASI), the military, and the domestic wool industry now indicate particular attention should be given to flame retardation or prevention to meet the needs of the military. Wool will ignite and burn with a self-extinguishing flame. To meet the needs of the military for itch-free, machine washable wool with improved burn-prevention behavior, we have developed a heat resistant polymer to
apply to ARS-processed wool fabric. The burning resistance of the treated fabric equals that of a wool/ Nomex fabric blend intended for military attire. The ARS product is preferred because it produces a soft crushable ash whereas the blend produces an intractable residue that can lodge in open wounds. ARS is introducing the military to comfortable, machine washable wool fabrics with improved flame retardancy (FR). This product will increase the demand for domestic wool fabrics that are processed entirely by textile mills in this country. This research concerns the apparel needs of the military in wartime and the textile industry recognizes that these developments will create novel commercial markets for wool. 1935-41440-014-02S-This report serves to document research conducted under a Specific Cooperative Agreement between ARS and the University of Georgia, which facilitated the work underwritten by base funds and Trust Fund Cooperative Agreement #58-1935-1-143 between ARS and
the American Sheep Industry Association (ASI; see report for 1935-41440-014-01T).Wool fibers are flammable but the propagating flame self-extinguishes and produces a soft ash residue unlike the melt-drip behavior of synthetic fibers that form a molten, hard bead upon cooling. Because of its self- extinguishing property, wool is used in airplane interiors and ARS- processed wool fabrics that overcome the itch-factor are preferred by the military to replace synthetic polypropylene underwear. To fully meet the flame retardant requirements for military attire, wool fiber is currently blended with Nomex or Kevlar (synthetic fibers known to resist burning). To improve the flame retardant properties of ARS-processed wool, a temperature-resistant, high-performance polymer that can be applied to wool fabric was synthesized. The burning resistance of the treated fabric equals that of a wool/ Nomex fabric blend intended for military attire. The polymer incorporates the highly ordered structure
of polyimide with soft segments of siloxanes to form nonignitable polyimidesiloxanes that are easy to process and exhibit thermal and radiation stability, stain and water resistance, and stability to UV light. Successful completion of this research will introduce the military to comfortable, machine- washable wool fabrics that will resist burning. To meet the military demand for these fabrics, participating wool mills are anticipated to include ERRC technology in their existing product lines, thereby increasing the demand for domestic wool fiber and apparel for traditional and new end uses. 5. Describe the major accomplishments over the life of the project, including their predicted or actual impact. This is the first annual report for this project. A major accomplishment is reported under question 4. 6. What science and/or technologies have been transferred and to whom? When is the science and/or technology likely to become available to the end- user (industry, farmer, other
scientists)? What are the constraints, if known, to the adoption and durability of the technology products? Functional modification of collagen: The collagen microfibril molecular model developed under previous projects is now providing a basis for research into the interactions of collagen with tannin-like molecules, and the effects of changes in ionic strength and pH on collagen by researchers in Europe. Functional modification of leather byproducts: Continued MOU with Dr. Karel Kolomaznik, Professor, Tomas Bata University, Zlin, Czech Republic in which the utilization of protein hydrolysate from waste leather products will be used to lower the formaldehyde content in resins. Developed a new MOU with Dr. Jaume Cot, Professor, Departamento de Ecotecnologias, CSIC, Barcelona, Spain for research on enzymatic modification of collagen by-products. Functional modification of wool: Mill trials of the process, patent pending, developed under Trust Fund Agreement 58-1935-1-143 with the
American Sheep Industry Association (ASI) , are being conducted under more than 20 individual confidentiality agreements with American wool mills. More than 20,000 pounds of wool fabric have been ARS-processed in finishing and dyeing plants throughout the country with plans to treat to treat raw wool fiber and wool yarns for commercial and handcrafter markets. One particular mill has applied the process continuously over the past year and is now petitioning to license with the intention to supply the military with itch-free, machine- washable wool for underwear. They are supplying the military with 10,000 ARS-processed undershirts for the first and second stages of wear trials by troops in the field. They plan to use the technology for private- sector products, for which the license is required. 7. List your most important publications in the popular press and presentations to organizations and articles written about your work. (NOTE: List your peer reviewed publications below).
Reports on the hides and leather phases of this project were presented to customers at the annual meeting of the Research Liaison Committee of the American Leather Chemists Association, ERRC, Wyndmoor, PA, April 26-27, 2005 (industry, academic, government representatives of the hides, leather, and tannery supplier industries). Progress reports on collaborative wool research with the American Sheep Industry Association (ASI) were prepared monthly for ASI review and presented in quarterly meetings at ERRC to an ASI representative. Collagen networks. In Leather Science and Engineering 15(1) 26-30 (in Chinese)
Impacts
(N/A)
Publications
- Gembeh, S.V., Farrell Jr, H.M., Taylor, M.M., Brown, E.M., Marmer, W.N. 2004. Application of transglutaminase to derivatize proteins. 1. studies on soluble proteins and preliminary results on wool. Journal of the Science of Food and Agriculture. 85:418-424.
- Taylor, M.M., Marmer, W.N., Brown, E.M. 2005. Characterization of biopolymers prepared from gelatin and sodium caseinate for potential use in leather processing. Journal of American Leather Chemists Association. 100(3):149-159.
- Taylor, M.M., Cabeza, L., Marmer, W.N., Brown, E.M. 2005. Preparation of high molecular weight products by crosslinking protein isolated from the enzymatic processing of chromium-containing collagenous waste i. extraction of gelatin. Leather Science and Engineering. 15(2):3-7.
- Brown, E.M. 2004. Potential interactions of the c-terminal telopeptides of bovine type i collagen. Journal of American Leather Chemists Association. 99(9):376-385.
- Lastowka, A.M., Brown, E.M., Maffia, G.J. 2005. A comparison of chemical, physical and enzymatic cross-linking of bovine type i collagen fibrils. Journal of American Leather Chemists Association. 100(5):196-202.
- Cardamone, J.M., Yao, J., Nunez, A. 2004. Controlling shrinkage in wool fabrics: effective hydrogen peroxide systems. Textile Research Journal. 74(10):887-898.
- Cardamone, J.M., Yao, J., Phillips, J.G. 2005. Combined bleaching, shrinkage prevention, and biopolishing of wool fabrics. Textile Research Journal. 75(2):169-174.
- Taylor, M.M., Bumanlag, L.P., Marmer, W.N., Brown, E.M. 2005. Preparation of fillers for leather from enzymatically modified collagen by-products [abstract]. American Leather Chemists Association. Paper No. 13.
- Kasala, J., Taylor, M.M., Raschik, P., Kolomaznik, K. 2005. Engineering study of collagen grafting [abstract]. American Leather Chemists Association. Paper No. 12.
- Brown, E.M., Stauffer, D.M., Cooke, P.H., Maffia, G.J. 2005. The effect of ultrasound on bovine hide collagen structure [abstract]. American Leather Chemists Association. Paper No. 14.
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