Characterization of functional intermediates of endoglucanase from Aspergillus aculeatus during urea and guanidine hydrochloride unfolding

Carbohydrate Research
Gajendra Sunnamada Naika, Purnima Kaul Tiku

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.

References

Mar 27, 2002·Acta Crystallographica. Section D, Biological Crystallography·Shahram KhademiEdgar F Meyer
Aug 10, 2007·Journal of Agricultural and Food Chemistry·Gajendra Sunnamada NaikaVishweshwaraiah Prakash

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Citations

Jun 10, 2011·Journal of Agricultural and Food Chemistry·Gajendra S Naika, Purnima Kaul Tiku
Jun 20, 2017·The FEBS Journal·Sai Krishna AndhirkaGopala Krishna Aradhyam
May 13, 2021·Journal of Biomolecular Structure & Dynamics·Tushar ChakrabortySubrata Sau

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