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Calcium-induced stabilization of α-amylase against guanidine hydrochloride denaturation


Citation

Tan, Cheau Yuaan and Raja Abdul Rahman, Raja Noor Zaliha and Abdul Kadir, Habsah and Tayya, Saad (2010) Calcium-induced stabilization of α-amylase against guanidine hydrochloride denaturation. African Journal of Biotechnology, 9 (46). art. no. 9903FE419346. pp. 7934-7941. ISSN 1684–5315

Abstract

Guanidine hydrochloride (GdnHCl) denaturation of native and Ca-depleted Bacillus licheniformis α-amylase (BLA) was investigated both in the absence and presence of 2 mM calcium chloride (CaCl2)using circular dichroism, fluorescence spectroscopy and biological activity. In both states (Cadepleted and native form), the protein was denatured to a considerable extent in the absence of 2 mM CaCl2 with concomitant loss of biological activity upon increasing GdnHCl concentration. On the other hand, this effect was significantly reduced when 2 mM CaCl2 was included in the incubation mixture as revealed by a higher relative mean residue ellipticity, higher relative fluorescence intensity, smaller change in emission maximum and lesser reduction in biological activity. Interestingly, using these probes, 2 mM CaCl2 seemed to offer the same degree of stability to Ca-depleted BLA as that observed with native BLA in the absence of 2 mM CaCl2. All these results suggest calcium-induced stabilization of BLA against GdnHCl denaturation.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Biotechnology and Biomolecular Sciences
Publisher: Academic Journals
Keywords: α-Amylase; Bacillus licheniformis; Calcium; Denaturation; Guanidine hydrochloride; Circular dichroism; Intrinsic fluorescence
Depositing User: Nida Hidayati Ghazali
Date Deposited: 12 Feb 2014 04:09
Last Modified: 13 Nov 2017 03:51
URI: http://psasir.upm.edu.my/id/eprint/13474
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