Please use this identifier to cite or link to this item: http://nopr.niscpr.res.in/handle/123456789/15268
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dc.contributor.authorLali, Arvind-
dc.contributor.authorManudhane, Kushal-
dc.contributor.authorMotlekar, Nuzhat-
dc.contributor.authorKarandikar, Priti-
dc.date.accessioned2012-12-22T19:57:45Z-
dc.date.available2012-12-22T19:57:45Z-
dc.date.issued2002-08-
dc.identifier.issn0975-0959 (Online); 0301-1208 (Print)-
dc.identifier.urihttp://hdl.handle.net/123456789/15268-
dc.description253-258en_US
dc.description.abstractImmobilized enzyme catalyzed biotransformations involving macromolecular substrates and/or products are greatly retarded due to slow diffusion of large substrate molecules in and out of the typical enzyme supports. Slow diffusion of macromolecules into the matrix pores can be speeded up by use of macroporous supports as enzyme carriers. Depolymerization reactions of polysaccharides like starch, pectin, and dextran to their respective low molecular weight products are some of the reactions that can benefit from use of such superporous matrices. In the present work, an indigenously prepared rigid cross-linked cellulose matrix (called CELBEADS) has been used as support for immobilizing alpha amylase (1,4-α-Dglucan glucanohydrolase, EC 3.2.1 . 1.) and pectinase (endo-PG: poly( 1 ,4-α-galactouronide) glycanohydrolase, EC 3.2. 1.1 5). The immobilized enzymes were used for starch and pectin hydrolysis respectively, in batch, packed bed and expanded bed modes. The macroporosity of CELBEADS was found to permit through-flow and easy diffusion of substrates pectin and starch to enzyme sites in the porous supports and gave reaction rates comparable to the rates obtained using soluble enzymes.en_US
dc.language.isoen_USen_US
dc.publisherNISCAIR, CSIRen_US
dc.rights CC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJBB Vol.39(4) [August 2002]en_US
dc.titleDepolymerization of starch and pectin using superporous matrix supported enzymesen_US
dc.typeArticleen_US
Appears in Collections:IJBB Vol.39(4) [August 2002]

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