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Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/877

Title: Simultaneous purification and immobilization of aspergillus niger xylanase on the reversibly soluble polymer eudragitTM L-100
Authors: Sardar, Meryam
Roy, Ipsita
Gupta, Munishwar N
Keywords: Xylanase
Cellulase-free immobilized xylanase
UV/Fluorescence/CD spectra of immobilized proteins
UV/Fluorescence/CD spectra of immobilized proteins
Non-covalent immobilization of enzymes
Water-soluble polymers
Issue Date: 2000
Citation: Enzyme and Microbial Technology, 27(9), 672–679
Abstract: The non-covalent immobilization of a commercial preparation of xylanase from A. niger was carried out on a reversibly soluble-insoluble enteric polymer EudragitTM L-100. The immobilization of the xylanase activity by adsorption was simultaneously accompanied by removal of cellulase activity since the latter did not bind to the polymer. Thus, the soluble enzyme derivative may be useful for treatment of paper pulp bleaching in paper industry. The immobilized xylanase retained 60% of its activity toward xylan as the substrate. No change was observed in the pH optimum (5.5) of the enzyme upon immobilization. Only marginal increase in the Km of the free enzyme (3.6 mg ml21 to 5.0 mg ml21) upon immobilization on the soluble polymer reflected that the enzyme-substrate binding continues to be efficient in spite of the macromolecular nature of the substrate. Fluorescence spectroscopy and UV difference spectroscopy were used to probe the change(s)in the enzyme structure upon immobilization. This change in structure was correlated with the effectiveness factor of the enzyme activity. CD spectra also showed that the enzyme undergoes drastic changes in the structure.
URI: http://eprint.iitd.ac.in/dspace/handle/2074/877
Appears in Collections:Chemistry

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