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

Agyei, Dominic and He, Lizhong 2015, Evaluation of cross-linked enzyme aggregates of Lactobacillus cell-envelope proteinases, for protein degradation, Food and bioproducts processing, vol. 94, pp. 59-69, doi: 10.1016/j.fbp.2015.01.004.

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Title Evaluation of cross-linked enzyme aggregates of Lactobacillus cell-envelope proteinases, for protein degradation
Author(s) Agyei, DominicORCID iD for Agyei, Dominic orcid.org/0000-0003-2280-4096
He, Lizhong
Journal name Food and bioproducts processing
Volume number 94
Start page 59
End page 69
Total pages 11
Publisher Elsevier
Place of publication Amsterdam, The Netherlands
Publication date 2015
ISSN 0960-3085
Keyword(s) Enzyme immobilization
Cross-linked enzyme aggregates (CLEAs)
Lactobacillus delbrueckii subsp. lactis313
Cell-envelope proteinases
Protein degradation
Peptide production
Summary Enzymatic hydrolysis is a widely used approach to improve the functional, nutritionaland physiological properties of food proteins. In this study, cross-linked enzyme aggre-gates (CLEAs) have been prepared from cell-envelope proteinases (CEPs) of Lactobacillusdelbrueckii subsp. lactis 313 and their proteolytic properties have been evaluated using severalfood proteins. We have optimized cross-linking conditions including ammonium sulphateconcentration, incubation temperatures, agitation speed, glutaraldehyde cross-linker con-centration, reaction time and the addition of proteic feeders. Particularly, the presence ofBSA 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 recyclabil-ity of CLCEPAs. CLCEPAs had attractive thermal stability at 50◦C and it showed enhancedcatalytic activity over long-term storage after lyophilization. We have demonstrated thatCLCEPAs has proteolytic properties on different food proteins including complex (chickenegg albumin, skimmed-milk protein), fractionated (bovine casein, whey protein isolate), andpurified (bovine serum albumin) proteins. Being the first report of CLEAs from lactobacilliCEPs, this study demonstrates the feasibility of using LDL 313 CLCEPAs for degradation ofvarious food proteins.
Language eng
DOI 10.1016/j.fbp.2015.01.004
Field of Research 100301 Biocatalysis and Enzyme Technology
100302 Bioprocessing, Bioproduction and Bioproducts
0904 Chemical Engineering
0908 Food Sciences
1003 Industrial Biotechnology
Socio Economic Objective 869899 Environmentally Sustainable Manufacturing not elsewhere classified
HERDC Research category C1.1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2015, Elsevier
Persistent URL http://hdl.handle.net/10536/DRO/DU:30074193

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