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Study on interaction of α-amylase from Bacillus subtilis with cetyl trimethylammonium bromide by Abdol-Khalegh Bordbar; Khodayar Omidiyan; Reza Hosseinzadeh is a Materials Science article available to read on EtoBox.

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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.

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Author

Abdol-Khalegh Bordbar; Khodayar Omidiyan; Reza Hosseinzadeh

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0927-7765)

Published

2005

Language

EN

Field

Materials Science (Physical Sciences)