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Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/332

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dc.contributor.authorSardar, M-
dc.contributor.authorAgarwal, R-
dc.contributor.authorA Kumar-
dc.contributor.authorGupta, M N-
dc.identifier.citationEnzyme and Microbial Technology, 20(5), 361-367en
dc.description.abstractThe noncovalent immobilization of enzymes such as alpha-amylase, beta-glucosidase, trypsin, and alkaline phosphatase was performed by adsorption on the water-soluble polymer Eudragit S-100. The strength of the binding with enzymes in some cases was critically dependent upon the initial polymer concentration used during binding. In all the cases tried, a moderate increase in polymer concentration ensured adequate immobilization of enzymes. The immobilized enzymes retained different activities: 87, 59, 49, and 24% for beta-glucosidase. alpha-amylase, trypsin, and alkaline phosphatase, respectively. The K, value of immobilized enzyme was the same as that of native enzyme for beta-glucosidase (3.8 x lo-’ M) and alpha-amylase (6 mg ml-‘) whereas the K, value decreased in the case of trypsin (from 1 x 10m3 M to 0.6 x lo-’ M) upon immobilization, The immobilized trypsin showed improved stability to autolysis at 35°C whereas immobilization resulted in a decrease in the thermal stability of alpha-amylase at 5O’C. No significant changes were observed in pH optimum of the enzymes upon immobilization. U.V. and fluorescence emission spectra of immobilized trypsin reflected the con-formational changes which enzymes undergo upon adsorption on the polymer.en
dc.format.extent286020 bytes-
dc.subjectalkaline phosphataseen
dc.subjectnoncovalent immobilization of enzymesen
dc.subjectimmobilized proteins;en
dc.subjectwater-soluble polymersen
dc.titleNoncovalent immobilization of enzymes on an enteric polymer eudragit S-100en
Appears in Collections:Chemistry

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