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Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/433

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dc.contributor.authorA Kumar-
dc.contributor.authorGupta, M N-
dc.date.accessioned2005-07-02T07:03:06Z-
dc.date.available2005-07-02T07:03:06Z-
dc.date.issued1998-
dc.identifier.citationJournal of molecular catalysis B enzymatic, 5, 289-294en
dc.identifier.urihttp://eprint.iitd.ac.in/dspace/handle/2074/433-
dc.description.abstractTrypsin was covalently linked to Eudragit S-100 an enteric coating polymer by carbodiimide coupling method. Nearly 90% of enzyme activity was conjugated to the polymer whereas actual observed expressed activity was 64%. The enzyme bound to the polymer by simple adsorption as well but leached off the polymer in the presence of high ionic strength (1.0 M NaCl)The immobilized enzyme showed stability to autolysis at 458C and had a marginal shift in pH optimum. The Km value of the enzyme decreased from 1.0=10y3 M to 0.7=10y3 M on immobilization. The soluble Eudragit-trypsin conjugate was used to hydrolyze casein at 458C. Eudragit being a reversibly soluble–insoluble polymer, the biocatalyst could be recovered and reused.en
dc.format.extent186774 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoenen
dc.subjectAutolysisen
dc.subjectCarbodiimide couplingen
dc.subjectCasein hydrolysisen
dc.subjectEudragiten
dc.subjectEudragit-trypsin conjugateen
dc.subjectTrypsinen
dc.subjectWater-soluble polymeren
dc.titleImmobilization of trypsin on an enteric polymer Eudragit S-100 for the biocatalysis of macromolecular substrateen
dc.typeArticleen
Appears in Collections:Biochemical Engg. and Biotechnology

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