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Poly-ε-lysine amylase conjugates to increase the stability of enzyme

Paper ID Volume ID Publish Year Pages File Format Full-Text
19708 43120 2014 6 PDF Available
Title
Poly-ε-lysine amylase conjugates to increase the stability of enzyme
Abstract

Poly-ε-lysine (ε-PL), an unusual naturally occurring homopolyamide of L-lysine having linkage between ε-amino and α-carboxyl groups, is biodegradable, edible and non-toxic towards human and environment. The conjugate of ε-PL with amylase was successfully prepared by ionic interaction. The ε-PL-amylase conjugate showed better temperature and pH stability than native enzyme. The degradation of enzyme by temperature and pH followed first order degradation kinetics. The k value (reaction constant), D value (decimal reduction time) and activation energy confirmed the better temperature stability of conjugated enzymes than native enzyme. The km and Vmax values were found to be similar for both conjugated and native enzyme suggesting, no change in enzyme configuration which alters the substrate binding.

Keywords
Poly-ε-lysine; Amylase; Conjugation; Degradation kinetics
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Poly-ε-lysine amylase conjugates to increase the stability of enzyme
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Publisher
Database: Elsevier - ScienceDirect
Journal: Food Bioscience - Volume 5, March 2014, Pages 85–90
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
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Any Questions? feel free to contact us