| Research Support Tool |
||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Immobilization of trypsin on an enteric polymer Eudragit S-100 for the biocatalysis of macromolecular substrate
Title:
Immobilization of trypsin on an enteric polymer Eudragit S-100 for the biocatalysis of macromolecular substrate
Archive:
Eprints@IIT Delhi
Author(s):
A Kumar
Gupta, M N
Gupta, M N
Date:
2005-07-02
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.
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.
Index terms:
Discipline(s):
Autolysis
Subject(s):
Carbodiimide coupling; Casein hydrolysis; Eudragit; Eudragit-trypsin conjugate; Trypsin; Water-soluble polymer
Method/Approach:
Coverage:
Publisher:
Contributors:
Source:
Language:
en
Relation:
Type:
Article
Format:
186774 bytes
application/pdf
Copyright Information: