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Chemical modification of wheat β-amylase by trinitrobenzenesulfonic acid, methoxypolyethylene glycol, and glutaraldehyde to improve its thermal stability and activity

Paper ID Volume ID Publish Year Pages File Format Full-Text
17073 42638 2013 7 PDF Available
Title
Chemical modification of wheat β-amylase by trinitrobenzenesulfonic acid, methoxypolyethylene glycol, and glutaraldehyde to improve its thermal stability and activity
Abstract

•The amino groups of wheat β-amylase (WBA) were chemically modified.•Methoxypolyethylene glycol (mPEG) improved the thermostability of WBA.•Glutaraldehyde (GA) improved the thermostability of WBA by 7 °C.•The thermostabilization by all chemical modifiers was entropy-driven.•WBA activity was increased by 39% by modification with mPEG.

The amino groups of wheat β-amylase (WBA) were modified by 2,4,6-trinitrobenzenesulfonic acid (TNBS), 2,4-bis (O-methoxypolyethylene glycol)-6-chloro-s-triazine (mPEG), and glutaraldehyde (GA) to improve its thermal stability and activity. Modification of WBA by 5 mM TNBS, 4.8 μM mPEG and 11 mM GA improved its T50 (the temperature at which 50% of its activity is lost after 30 min of incubation) from 47 ± 1 °C to 48 ± 2, 55 ± 2, and 54 ± 2 °C, respectively. The catalytic activity of WBA was reduced by 15% and 59% with modification by 5 mM TNBS and 11 mM GA, respectively. In all cases, the enhancement of thermostability of modified WBA was entropically driven. The activity of WBA modified by 4.8 μM mPEG was enhanced by 39% at 25 °C. Therefore, the thermal stability of WBA was significantly improved by modification with mPEG, GA and slightly by TNBS and its catalytic activity was enhanced by mPEG.

Keywords
Amino groups; Chemical modification; Catalytic activity; Thermal inactivation; Wheat β-amylaseBA, β-amylase; GA, glutaraldehyde; mPEG, 2,4-bis (O-methoxypolyethylene glycol)-6-chloro-s-triazine; TNBS, 2,4,6-trinitrobenzenesulfonic acid; WBA, wheat β-amyla
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Chemical modification of wheat β-amylase by trinitrobenzenesulfonic acid, methoxypolyethylene glycol, and glutaraldehyde to improve its thermal stability and activity
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 53, Issues 6–7, 10 December 2013, Pages 420–426
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