@article{bb2014222,
author={{Miroliaei, Mehran and Sharifi, Rasoul and Halling, Peter J.},
title={Three Diverse Alcohol Dehydrogenases Remain Active at Salt Concentrations Greater than 1 M},
journal={Biomedicine and Biotechnology},
volume={2},
number={2},
pages={37--41},
year={2014},
url={http://pubs.sciepub.com/bb/2/2/2},
issn={2328-4137},
abstract={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 > Na<SUB>2</SUB>SO<SUB>4</SUB> > NaNO<SUB>3</SUB> > NaClO<SUB>4</SUB>. The deviation from the normal Hofmeister series may reflect effects in line with the ˇ°law of matching water affinityˇ±, based on anion interactions with the Na<SUP>+</SUP> cation in solution or the essential Zn<SUP>2+</SUP> 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<SUP>+</SUP>, K<SUP>+</SUP>, NH<SUP>4+</SUP> and Na<SUP>+</SUP> showed weaker effects, not clearly in line with the Hofmeister series.},
doi={10.12691/bb-2-2-2}
publisher={Science and Education Publishing}
}