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Evaluation of cross-linked enzyme aggregates of Lactobacillus cell-envelope proteinases, for protein degradation

Version 2 2024-06-07, 00:29
Version 1 2015-07-09, 12:18
journal contribution
posted on 2024-06-07, 00:29 authored by D Agyei, L He
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 delbrueckii 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 con-centration, 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.

History

Journal

Food and bioproducts processing

Volume

94

Article number

C

Pagination

59-69

Location

Amsterdam, The Netherlands

ISSN

0960-3085

Language

eng

Publication classification

C Journal article, C1.1 Refereed article in a scholarly journal

Copyright notice

2015, Elsevier

Publisher

Elsevier