Enhanced stability of alcohol dehydrogenase by non-covalent interaction with polysaccharides.

Abstract:

:Non-covalent interaction of alcohol dehydrogenase with polysaccharides was studied using three neutral and three anionic polysaccharides. The process of interaction of alcohol dehydrogenase with gum Arabic was optimized with respect to the ratio of enzyme to gum Arabic, pH, and molarity of buffer. Alcohol dehydrogenase-gum Arabic complex formed under optimized conditions showed 93% retention of original activity with enhanced thermal and pH stability. Lower inactivation rate constant of alcohol dehydrogenase-gum Arabic complex within the temperature range of 45 to 60 °C implied its better stability. Half-life of alcohol dehydrogenase-gum Arabic complex was higher than that of free alcohol dehydrogenase. A slight increment was observed in kinetic constants (K(m) and V(max)) of gum Arabic-complexed alcohol dehydrogenase which may be due to interference by gum Arabic for the binding of substrate to the enzyme. Helix to turn conversion was observed in complexed alcohol dehydrogenase as compared to free alcohol dehydrogenase which may be responsible for observed stability enhancement.

authors

Jadhav SB,Bankar SB,Granström T,Ojamo H,Singhal RS,Survase SA

doi

10.1007/s00253-014-5579-9

subject

Has Abstract

pub_date

2014-01-01 00:00:00

pages

6307-16

issue

14

eissn

0175-7598

issn

1432-0614

journal_volume

98

pub_type

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