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Interaction of carbohydrates with alcohol dehydrogenase: Effect on enzyme activity

Paper ID Volume ID Publish Year Pages File Format Full-Text
20184 43162 2015 5 PDF Available
Title
Interaction of carbohydrates with alcohol dehydrogenase: Effect on enzyme activity
Abstract

•Oxidized glucose, starch and pectin inhibited alcohol dehydrogenase.•Inhibition rate constant increased with an increase in concentration of carbohydrates.•Thiol groups of enzyme were involved in binding with inhibitiors.•Oxidized pectin was the most potent inhibitors among the carbohydrates studied.

Alcohol dehydrogenase was covalently conjugated with three different oxidized carbohydrates i.e., glucose, starch and pectin. All the carbohydrates inhibited the enzyme. The inhibition was studied with respect to the inhibition rate constant, involvement of thiol groups in the binding, and structural changes in the enzyme. The enzyme activity decreased to half of its original activity at the concentration of 2 mg/mL of pectin, 4 mg/mL of glucose and 10 mg/mL of starch within 10 min at pH 7. This study showed oxidized pectin to be a potent inhibitor of alcohol dehydrogenase followed by glucose and starch. Along with the aldehyde-amino group interaction, thiol groups were also involved in the binding between alcohol dehydrogenase and carbohydrates. The structural changes occurring on binding of alcohol dehydrogenase with oxidized carbohydrates was also confirmed by fluorescence spectrophotometry. Oxidized carbohydrates could thus be used as potential inhibitors of alcohol dehydrogenase.

Keywords
Alcohol dehydrogenase; Carbohydrates; Inhibition; Thiol groups; Covalent binding
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 120, Issue 3, September 2015, Pages 252–256
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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