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Please use this identifier to cite or link to this item: http://dyuthi.cusat.ac.in/purl/2264

Title: Acid activated montmorillonite: an efficient immobilization support for improving reusability, storage stability and operational stability of enzymes
Authors: Sanjay, Gopinath
Sugunan, S
Science
Keywords: α-Amylase
Glucoamylase
Invertase
Immobilization
Montmorillonite
Adsorption
Covalent binding
Issue Date: 2008
Publisher: Springer Netherlands
Abstract: Three enzymes, α-amylase, glucoamylase and invertase, were immobilized on acid activated montmorillonite K 10 via two independent techniques, adsorption and covalent binding. The immobilized enzymes were characterized by XRD, N2 adsorption measurements and 27Al MAS-NMR spectroscopy. The XRD patterns showed that all enzymes were intercalated into the clay inter-layer space. The entire protein backbone was situated at the periphery of the clay matrix. Intercalation occurred through the side chains of the amino acid residues. A decrease in surface area and pore volume upon immobilization supported this observation. The extent of intercalation was greater for the covalently bound systems. NMR data showed that tetrahedral Al species were involved during enzyme adsorption whereas octahedral Al was involved during covalent binding. The immobilized enzymes demonstrated enhanced storage stability. While the free enzymes lost all activity within a period of 10 days, the immobilized forms retained appreciable activity even after 30 days of storage. Reusability also improved upon immobilization. Here again, covalently bound enzymes exhibited better characteristics than their adsorbed counterparts. The immobilized enzymes could be successfully used continuously in the packed bed reactor for about 96 hours without much loss in activity. Immobilized glucoamylase demonstrated the best results.
URI: http://dyuthi.cusat.ac.in/purl/2264
ISSN: 1380-2224
Appears in Collections:Dr. Sugunan S

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