Abstract
Purified endoglucanase from C. biazotea mutant 51SMr was successfully immobilized on Eudragit L-100, with 75 % yield of immobilization. This method improved the kinetic and thermodynamic properties of the enzyme. Immobilization significantly decreased entropy and enthalpy of inactivation of biocatalyst and made it functionally and thermodynamically more stable and reusable compared to free one.
Keywords: Eudragit L-100, immobilization kinetics, melting point, substrate binding energy, thermodynamics, transition state stabilization
Protein & Peptide Letters
Title: A Surface Immobilization Method of Endoglucanase from Cellulomonas biazotea Mutant Improved Catalytic Properties of Biocatalyst During Processing
Volume: 14 Issue: 7
Author(s): Muhammad Ibrahim Rajoka, Yasmin Zia and Khalil-ur-Rehman
Affiliation:
Keywords: Eudragit L-100, immobilization kinetics, melting point, substrate binding energy, thermodynamics, transition state stabilization
Abstract: Purified endoglucanase from C. biazotea mutant 51SMr was successfully immobilized on Eudragit L-100, with 75 % yield of immobilization. This method improved the kinetic and thermodynamic properties of the enzyme. Immobilization significantly decreased entropy and enthalpy of inactivation of biocatalyst and made it functionally and thermodynamically more stable and reusable compared to free one.
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Cite this article as:
Muhammad Ibrahim Rajoka , Yasmin Zia and Khalil-ur-Rehman , A Surface Immobilization Method of Endoglucanase from Cellulomonas biazotea Mutant Improved Catalytic Properties of Biocatalyst During Processing, Protein & Peptide Letters 2007; 14 (7) . https://dx.doi.org/10.2174/092986607781483886
DOI https://dx.doi.org/10.2174/092986607781483886 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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