1Developmental and Molecular Biology Division, Department of Biology, Faculty of Sciences, University of Isfahan, Isfahan, Iran
2Department of Biology, Research and Science Branch, Islamic Azad University, Tehran, Iran
3WestCHEM, Department of Pure & Applied Chemistry, University of Strathclyde, Glasgow G1 1XL, UK
Biomedicine and Biotechnology.
2014,
Vol. 2 No. 2, 37-41
DOI: 10.12691/bb-2-2-2
Copyright © 2014 Science and Education PublishingCite this paper: Mehran Miroliaei, Rasoul Sharifi, Peter J. Halling. Three Diverse Alcohol Dehydrogenases Remain Active at Salt Concentrations Greater than 1 M.
Biomedicine and Biotechnology. 2014; 2(2):37-41. doi: 10.12691/bb-2-2-2.
Correspondence to: Mehran Miroliaei, Developmental and Molecular Biology Division, Department of Biology, Faculty of Sciences, University of Isfahan, Isfahan, Iran. Email:
mmiroliaei@yahoo.comAbstract
A comparative study was carried out on the effects of a number of salts on enzyme activity of three representative alcohol dehydrogenases from non-halophilic sources. The enzymes from yeast (YADH), horse liver (HLADH) and Thermoanaerobacter brockii (TBADH) all retain significant activity at concentrations up to 4 M NaCl. In general catalytic activity follows the order NaCl > Na-acetate > Na2SO4 > NaNO3 > NaClO4. The deviation from the normal Hofmeister series may reflect effects in line with the “law of matching water affinity”, based on anion interactions with the Na+ cation in solution or the essential Zn2+ in the enzymes. Retention of activity generally follows the order YADH > HLADH > TBADH, which is opposite to the order of thermostability. Protein structural features promoting thermostability, like additional salt bridges, may lead to greater salt sensitivity. Comparison of cations Cs+, K+, NH4+ and Na+ showed weaker effects, not clearly in line with the Hofmeister series.
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