Progress 10/26/17 to 09/30/18
Outputs
Target Audience:
Nothing Reported
Changes/Problems:
Nothing Reported
What opportunities for training and professional development has the project provided? One Master-level graduate students completed her thesis research through this project. She will graduate in May 2019. Two undergraduate students and two dietetic interns were involved in the project to obtain hand-on training. They presented their findings at the professional meetings, and are co-authors in a refereed publication. How have the results been disseminated to communities of interest?The finding has been submitted for publication in peer-reviewed journal and has been presented at the professional meetings What do you plan to do during the next reporting period to accomplish the goals?During next reporting period, we plan to comprehensively characterize functional, structural and biological activities of produced peptides
Impacts
What was accomplished under these goals?
The 'Year 1' study objective was to determine optimal enzymatic hydrolysis condition for production of bioactive peptides from isolated chickpea proteins. We investigated the effects of different hydrolysis processing, using Alcalase and Flavourzyme individually or sequential treatment by initial Alacase followed by Flavourzyme), onbfunctional, structural and antioxidant properties as well as SDS-PAGE profiles of the hydrolysates. Alcalase was more effective than Flavourzyme to cleave the peptide bonds, and Alcalase-treated hydrolysate had a degree of hydrolysis (DH) of 26%. Extensive hydrolysis occurred during sequential treatment, and DH of sequentially-treated hydrolysates reached up to 50%. Although hydrolysis processing significantly (P<0.05) increased emulsifying capacity of protein, the sequentially-treated hydrolysates exhibited a lower emulsifying capacity than their single enzyme-treated counterparts. FTIR results indicated that original chickpea proteins had a dominant β-sheet secondary structure (60.4%). Hydrolysis caused a pronounced loss of ordered secondary structures including β-sheet and α-helix, but a significant increase in β-turn and formation of a new random coil structure, especially for those that were hydrolyzed sequentially which had highest β-turn (42.9%) and lowest ratio of β-sheet (29.2%) and α-helix (15.0%). During the hydrolysis, SDS banding pattern markedly changed, especially for those treated by Alcalase either individually or sequentially which did not show any visible protein bands. Compared to original chickpea protein isolate, all hydrolyzates presented significantly (P<0.05) higher DPPH• scavenging capacity, especially sequentially-treated hydrolysates had more potent in scavenging DPPH• radicals. The results reveal that hydrolysis promoted functional properties and antioxidant activity of protein for potential functional food ingredient application
Publications
- Type:
Journal Articles
Status:
Submitted
Year Published:
2018
Citation:
Yixiang Xu, Magdalini Galanopoulos, Edward Sismour, Shuxin Ren, Zelalem Mersha, Patricia Lynch, Abeer Almutaimi. 2018. International Journal of food Science & Technology, Functional, structural, and antioxidant properties of chickpea protein hydrolysates affected by enzymatic hydrolysis.
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