Effect of aniline coupling on kinetic and thermodynamic properties of Fusarium solani glucoamylase |
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Authors: | Haq Nawaz Bhatti M Hamid Rashid Rakhshanda Nawaz A Mukhtar Khalid Muhammad Asgher A Jabbar |
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Institution: | (1) Department of Chemistry, University of Agriculture, Faisalabad, 38040, Pakistan;(2) National Institute for Biotechnology and Genetic Engineering (NIBGE), P.O. Box 577, Jhang road, Faisalabad, Pakistan |
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Abstract: | Purified glucoamylase (GA) from Fusarium solani was chemically modified by cross-linking with aniline hydrochloride in the presence of 1-ethyl-3-(3-dimethylaminopropyl)
carbodiimide (EDC) for 1 aniline-coupled glucoamylase-1 (ACG-1)], 7 (ACG-7), and 13 min (ACG-13). The aniline coupling of
GA had a profound enhancing effect on temperature, pH optima, and pK
a’s of active site residues. The specificity constants (K
cat/K
m) of native, ACG-1, ACG-7, and ACG-13 were 136, 244, 262, and 208 at 55°C for starch, respectively. The enthalpy of activation
(ΔH*) and free energy of activation (ΔG*) for soluble starch hydrolysis were lower for the chemically modified forms compared to native GA. Proteolysis of ACGs by
α-chymotrypsin and subtilisin resulted in activation. |
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Keywords: | Glucoamylase Carboxylic group modification Fusarium solani Enthalpy Free energy Thermostability |
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