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Cross-linking enzyme aggregates in the macropores of silica gel: A practical and efficient method for enzyme stabilization

Paper ID Volume ID Publish Year Pages File Format Full-Text
3886 197 2010 7 PDF Available
Title
Cross-linking enzyme aggregates in the macropores of silica gel: A practical and efficient method for enzyme stabilization
Abstract

Cross-linked enzyme aggregates of papain were prepared in commercial macroporous silica gel (CLEAs-MSG) in order to improve the operability and mechanical stability of CLEAs. CLEAs-MSG was obtained from simple adsorption, precipitation and one-step-cross-linking. CLEAs-MSG was characterized by stable structure that did not leak out enzyme from the macropores because of covalent bonding between CLEAs and MSG. The optimal temperature of papain CLEAs in MSG was 40–90 °C and the optimal pH was 7.0, which were improved compared to free papain and CLEAs. The CLEAs-MSG also enhanced the storage stability and thermal stability. Moreover, the CLEAs-MSG exhibited good reusability due to its suitable size and active properties. By using CLEAs-MSG of papain as biocatalyst, the kinetically controlled z-Ala-Gln synthesis was achieved with the yield of 32.9%, which was almost equal to that by using free papain as biocatalyst.

Keywords
Enzyme; Immobilization; CLEAs (cross-linked enzyme aggregates); Macroporous silica gel; Dipeptide synthesis; Papain
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 52, Issues 2–3, 15 November 2010, Pages 168–174
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us