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A Surface Immobilization Method of Endoglucanase from Cellulomonas biazotea Mutant Improved Catalytic Properties of Biocatalyst During Processing

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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

Document Type: Research Article


Publication date: 2007-07-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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