Journal ArticleDOI
Enhanced stability of alcohol dehydrogenase by non-covalent interaction with polysaccharides
Swati B. Jadhav,Sandip B. Bankar,Tom Granström,Heikki Ojamo,Rekha S. Singhal,Shrikant A. Survase +5 more
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TLDR
Alcohol dehydrogenase–gum Arabic complex formed under optimized conditions showed 93 % retention of original activity with enhanced thermal and pH stability and Helix to turn conversion was observed in complexed alcohol dehydration as compared to free alcohol dehydrogen enzyme which may be responsible for observed stability enhancement.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.read more
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Catalytic, kinetic and thermodynamic properties of stabilized Bacillus stearothermophilus alkaline protease.
TL;DR: The enzyme proved to be metalloprotease and significantly stimulated by Ca2+ and Mg2+ whereas Hg2+, Fe3+ Cu2- and Zn2+ inhibited the enzyme activity and there was no pronounced effect on substrate specificity after conjugation.
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Improving the catalytic, kinetic and thermodynamic properties of Bacillus subtilis KU710517 milk clotting enzyme via conjugation with polyethylene glycol
Hala Refaat Wehaidy,Mohamed A. Abdel-Naby,Wafaa Ghoneim Shousha,Mohammed I. Y. Elmallah,Michael Mounir Shawky +4 more
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Macromolecular crowding and the steady-state kinetics of malate dehydrogenase.
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Surface modification of polysulfone membranes applied for a membrane reactor with immobilized alcohol dehydrogenase
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Enhanced thermal stability and pH behavior of glucose oxidase on electrostatic interaction with polyethylenimine.
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References
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Complex coacervation of proteins and anionic polysaccharides
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C. G. de Kruif,Remco Tuinier +1 more
TL;DR: In this article, the interaction between proteins and polysaccharides, as can be observed in food related systems, is systematically discussed by separating biopolymer interactions into respectively enthalpy- and entropy-dominated types.
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Protein-polysaccharide interactions: phase-ordering kinetics, thermodynamic and structural aspects
TL;DR: The most important parameters affecting protein-polysaccharide interactions are now well documented, and recent advances concern the structure-building kinetics, thermodynamics and structure of mixtures as mentioned in this paper.
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Recent advances in the biocatalytic reduction of ketones and oxidation of sec-alcohols.
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