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Does Recovery in the Spectral Characteristics of GdnHCl-Denatured Bacillus licheniformis α-Amylase Due to Added Calcium Point towards Protein Stabilization?
MedLine Citation:
PMID:  23291750     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Treatment of Bacillus licheniformis α-amylase (BLA) with guanidine hydrochloride (GdnHCl) produced both denatured and aggregated forms of the enzyme as studied by circular dichroism, fluorescence, UV difference spectroscopy, size exclusion chromatography (SEC), and enzymatic activity. The presence of CaCl(2) in the incubation mixture produced significant recovery in spectral signals, being complete in presence of 10 mM CaCl(2), as well as in enzymatic activity, which is indicative of protein stabilization. However, the SEC results obtained with GdnHCl-denatured BLA both in the absence and the presence of 10 mM CaCl(2) suggested significant aggregation of the protein in the absence of CaCl(2) and disaggregation in its presence. Although partial structural stabilization with significant retention of enzymatic activity was observed in the presence of calcium, it was far from the native state, as reflected by spectral probes. Hence, spectral results as to BLA stabilization should be treated with caution in the presence of aggregation.
Authors:
Adyani Azizah Abd Halim; Shevin Rizal Feroz; Saad Tayyab
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-07
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  -     ISSN:  1347-6947     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-7     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Biomolecular Research Group, Biochemistry Programme, Institute of Biological Sciences, Faculty of Science, University of Malaya.
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