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

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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.

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Authors and Affiliations

  1. Department of Biotechnology and Chemical Technology, School of Chemical Technology, Aalto University, POB 16100, 00076, Aalto, Finland

    Swati B. Jadhav, Sandip B. Bankar, Tom Granström, Heikki Ojamo & Shrikant A. Survase

  2. Food Engineering and Technology Department, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga, Mumbai, 400 019, India

    Swati B. Jadhav & Rekha S. Singhal

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  1. Swati B. Jadhav
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  2. Sandip B. Bankar
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  3. Tom Granström
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  4. Heikki Ojamo
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  5. Rekha S. Singhal
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  6. Shrikant A. Survase
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Correspondence to Shrikant A. Survase.

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Jadhav, S.B., Bankar, S.B., Granström, T. et al. Enhanced stability of alcohol dehydrogenase by non-covalent interaction with polysaccharides. Appl Microbiol Biotechnol 98, 6307–6316 (2014). https://doi.org/10.1007/s00253-014-5579-9

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  • DOI: https://doi.org/10.1007/s00253-014-5579-9

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