Progress 10/01/06 to 09/30/11
Outputs
OUTPUTS: Commercial feather meal is of low value because of its poor digestibility. Meat and bone meal is banned because of the scare of contamination of prion protein that may cause mad cow disease. Keratinase is known to be able to degrade feathers and prions. It will be incoporated into the processes to produce more digestible feather meal and prion-free meat and bone meal. Objectives were to: 1) develop an enzymatic process to produce feather meal of improved digestibility and nutritional quality and 2)to develop an enzymatic disinfection process to produce prion-free meat and bone meal, using prion-like protein as the marker. PARTICIPANTS: Mr. Brian Spencer, Research Specialist, NCSU Dr. Jason Shih, NCSU Dr. Jeng-Jie Wang, CSO of BioResource International, Inc. TARGET AUDIENCES: Animal and poultry industries. Bio-industries who are interested in enzyme applications. PROJECT MODIFICATIONS: Not relevant to this project.
Impacts
The purpose of the study of enzymatic process for feather meal cooking is to find out the optimun conditions to produce a value-added feather meal. When the keratinase based cooking is established, the method will improve the utilization and upgrade the value of feathers, the major by-product of poultry industry. The study of enzymatic degradation of prion protein is of great importance in protecting food safety. Meat and bone meal, as derived from beed industry, is of great concern for its potential contaimination of prions. Prion protein is the putative causative agent of bovine spongiform encephalopathy (BSE), or commonly known as mad cow disease.
Publications
- Wang, J.J., Borwornpinyo, R. and Shih, J.C.H. (2007) Sup35NM-His6 aggregate: a prion-like protein useful in prion degradation studies. Enz. Microb. Technol. 40:976-981.
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Progress 10/01/06 to 09/30/07
Outputs
OUTPUTS: Keratinase is being tested for its activity in processing feather meal. Most of the time was trying to set up the optimun conditions, cooking time and temperature, enzymatic treatment prior to or post the cooking. The processed feather meal is being evaluated for its digestibility and nutritional value. Different methods were used, including pepsin digestibility, soluble proteins, amino acid analysis and animal feeding test. The optimun conditions and the prefered method(s) for analysis are being studied and has not been finalized. Keratinase degradation of prion protein was studied using a prion-like surrogate protein, Sup35NM-His6, as the marker. Optimun enzyme concentrations and incubation conditions have been determined, as monitored by Western blotting. The enzymatic method was compared with known sterilizing methods such as cooking with NaOH or hypochlorite.
PARTICIPANTS: Individual: Dr. Jeng-Jie Wang, CSO of BioResource International, Inc. Mr. Brian Spencer, Research Specialist, NCSU. Organization: BioResource International, Inc. Training: This project hires part-time studuents at NCSU to assist and to learn.
TARGET AUDIENCES: Animal and poultry industries. Bio-industries who are interested in enzyme applications.
PROJECT MODIFICATIONS: None.
Impacts
The purpose of the study of enzymatic process for feather meal cooking is to find out the optimun conditions to produce a value-added feather meal. When the keratinase based cooking is established, the method will improve the utilization and upgrade the value of feathers, the major by-product of poultry industry. The study of enzymatic degradation of prion protein is of great importance in protecting food safety. Meat and bone meal, as derived from beed industry, is of great concern for its potential contaimination of prions. Prion protein is the putative causative agent of bovine spongiform encephalopathy (BSE), or commonly known as mad cow disease.
Publications
- Wang, J.J., Borwornpinyo, R. and Shih, J.C.H. (2007) Sup35NM-His6 aggregate: a prion-like protein useful in prion degradation studies. Enz. Microb. Technol. 40:976-981.
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