alexa Characterization of functional intermediates of endoglucanase from Aspergillus aculeatus during urea and guanidine hydrochloride unfolding.
Environmental Sciences

Environmental Sciences

Journal of Bioremediation & Biodegradation

Author(s): Naika GS, Tiku PK

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Abstract Low concentrations of urea and GuHCl (2 M) enhanced the activity of endoglucanase (EC 3.1.2.4) from Aspergillus aculeatus by 2.3- and 1.9-fold, respectively. The K(m) values for controls, in the presence of 2 M urea and GuHCl, were found to be 2.4 +/- 0.2 x 10(-8) mol L(-1), 1.4 +/- 0.2 x 10(-8) mol L(-1), and 1.6 +/- 0.2 x 10(-8) mol L(-1), respectively. The dissociation constant (Kd) showed changes in the affinity of the enzyme for the substrate with increases in the Kcat suggesting an increased turnover number in the presence of urea and GuHCl. Fluorescence studies showed changes in the microenvironment of the protein. The increase in the activity of this intermediate state was due to conformational changes accompanied by increased flexibility at the active site. This article was published in Carbohydr Res and referenced in Journal of Bioremediation & Biodegradation

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