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Quick and low cost immobilization of proteinases on polyesters: comparison of lactobacilli cell-envelope proteinase and trypsin for protein degradation

Agyei,D, Tambimuttu,S, Kasargod,B, Gao,Y and He,L 2014, Quick and low cost immobilization of proteinases on polyesters: comparison of lactobacilli cell-envelope proteinase and trypsin for protein degradation, Journal of biotechnology, vol. 188, pp. 53-60, doi: 10.1016/j.jbiotec.2014.08.007.

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Title Quick and low cost immobilization of proteinases on polyesters: comparison of lactobacilli cell-envelope proteinase and trypsin for protein degradation
Author(s) Agyei,DORCID iD for Agyei,D orcid.org/0000-0003-2280-4096
Tambimuttu,S
Kasargod,B
Gao,Y
He,L
Journal name Journal of biotechnology
Volume number 188
Start page 53
End page 60
Total pages 8
Publisher Elsevier
Place of publication Amsterdam, The Netherlands
Publication date 2014-10-20
ISSN 1873-4863
Keyword(s) Cell-envelope proteinase
Enzyme immobilization
Lactobacilli
Polyester fabric
Protein degradation
Summary Cell-envelope proteinases (CEPs) are a class of proteolytic enzymes produced by lactic acid bacteria and have several industrially relevant applications. However, soluble CEPs are economically unfavorable for such applications due to their poor stability and lack of reusability. In a quest to prepare stable biocatalysts with improved performance, CEP from Lactobacillus delbrueckii subsp. lactis 313 and trypsin (as a model enzyme) were immobilized onto nonwoven polyester fabrics in a three-step protocol including ethylenediamine activation and glutaraldehyde crosslinking. Immobilization gave protein loading yields of 21.9% (CEP) and 67.7% (trypsin) while residual activity yields were 85.6% (CEP) and 4.1% (trypsin). The activity of the immobilized enzymes was dependent on pH, but was retained at elevated temperatures (40-70°C). An increase in Km values was observed for both enzymes after immobilization. After 70 days of storage, the immobilized CEP retained ca. 62% and 96% of initial activity when the samples were stored in a lyophilized form at -20°C or in a buffer at 4°C, respectively. Both immobilized CEP and trypsin were able to hydrolyze proteins such as casein, skimmed milk proteins and bovine serum albumin. This immobilization protocol can be used to prepare immobilized biocatalyst for various protein degradation processes.
Language eng
DOI 10.1016/j.jbiotec.2014.08.007
Field of Research 100302 Bioprocessing, Bioproduction and Bioproducts
091209 Polymers and Plastics
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 ©2014, Elsevier
Persistent URL http://hdl.handle.net/10536/DRO/DU:30072770

Document type: Journal Article
Collection: School of Life and Environmental Sciences
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