| Literature DB >> 15620842 |
Abdol-Khalegh Bordbar1, Khodayar Omidiyan, Reza Hosseinzadeh.
Abstract
The interaction of cetyl trimethylammonium bromide (CTAB) with alpha-amylase from Bacillus subtilis was investigated at 25 degrees C and various experimental conditions, such as pH, ionic strength and urea concentration. The binding data were measured using CTAB-membrane selective electrodes as a simple, fast, cheap and accurate method. The obtained binding isotherms were analyzed using Wyman binding potential concept. The results represent the highest binding affinity at 10(-3) M of NaBr respect to other salt concentrations. The less binding affinity at pH 9.7 with respect to pH 6.5 is related to increasing of protein self aggregation with pH. The binding data analysis at various urea concentrations also shows that the predominate unfolding of alpha-amylase occurred in the urea concentration range of 3-5 M.Entities:
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Year: 2005 PMID： 15620842 DOI： 10.1016/j.colsurfb.2004.10.002
Source DB: PubMed Journal: Colloids Surf B Biointerfaces ISSN： 0927-7765 Impact factor: 5.268