EPrints@IIT Delhi : Item 2074/433

Please use this identifier to cite or link to this item: http://hdl.handle.net/2074/433

Full metadata record

DC Field	Value	Language
contributor.author	A Kumar	-
contributor.author	Gupta, M N	-
date.accessioned	2005-07-02T07:03:06Z	-
date.available	2005-07-02T07:03:06Z	-
date.issued	1998	-
identifier.citation	Journal of molecular catalysis B enzymatic, 5, 289-294	en
identifier.uri	http://eprint.iitd.ac.in/dspace/handle/2074/433	-
description.abstract	Trypsin 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
format.extent	186774 bytes	-
format.mimetype	application/pdf	-
language.iso	en	en
subject	Autolysis	en
subject	Carbodiimide coupling	en
subject	Casein hydrolysis	en
subject	Eudragit	en
subject	Eudragit-trypsin conjugate	en
subject	Trypsin	en
subject	Water-soluble polymer	en
title	Immobilization of trypsin on an enteric polymer Eudragit S-100 for the biocatalysis of macromolecular substrate	en
type	Article	en
Appears in Collections:	Biochemical Engg. and Biotechnology

Files in This Item:

File	Description	Size	Format
kumarimm98.pdf		182Kb	Adobe PDF	View/Open