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- Title
Evaluation of cross-linked enzyme aggregates of Lactobacillus cell-envelope proteinases, for protein degradation.
- Authors
Agyei, Dominic; Lizhong He
- Abstract
Enzymatic hydrolysis is a widely used approach to improve the functional, nutritional and physiological properties of food proteins. In this study, cross-linked enzyme aggregates (CLEAs) have been prepared from cell-envelope proteinases (CEPs) of Lactobacillus delbruecfeii subsp. lactis 313 and their proteolytic properties have been evaluated using several food proteins. We have optimized cross-linking conditions including ammonium sulphate concentration, incubation temperatures, agitation speed, glutaraldehyde cross-linker concentration, reaction time and the addition of proteic feeders. Particularly, the presence of BSA improves retained activity of cross-linked CEP aggregates (CLCEPAs) from 21.5% to 40.9%. Blocking unreacted cross-linking groups on aggregates is important to enhance recyclability of CLCEPAs. CLCEPAs had attractive thermal stability at 50 °C and it showed enhanced catalytic activity over long-term storage after lyophilization. We have demonstrated that CLCEPAs has proteolytic properties on different food proteins including complex (chicken egg albumin, skimmed-milk protein), fractionated (bovine casein, whey protein isolate), and purified (bovine serum albumin) proteins. Being the first report of CLEAs from lactobacilli CEPs, this study demonstrates the feasibility of using LDL 313 CLCEPAs for degradation of various food proteins.
- Subjects
PLANT enzyme regulation; ENZYME regulation; HYDROLYSIS; BIODEGRADATION; LACTOBACILLUS; PROTEINASE regulation; PHYSIOLOGY
- Publication
Food & Bioproducts Processing: Transactions of the Institution of Chemical Engineers Part C, 2015, Vol 94, p59
- ISSN
0960-3085
- Publication type
Article
- DOI
10.1016/j.fbp.2015.01.004