作者: A Zaks , A M Klibanov
DOI: 10.1016/S0021-9258(18)68435-2
关键词:
摘要: Three model, unrelated enzymes (yeast alcohol oxidase, mushroom polyphenol and horse liver dehydrogenase) were found to be catalytically active in a variety of organic solvents. For all solvents tested, the enzymatic activity greatly increased upon an increase water content (which always remained below solubility limit). Much less was required reach maximal hydrophobic than their hydrophilic counterparts. However, when catalytic plotted versus amount bound enzymes, common pattern emerged for different These data suggest that effect on enzyme is primarily due interactions with enzyme-bound, essential layer rather itself. At optimal contents, activities range from 20 40% those aqueous solutions. From experiments (i) replacement other hydrogen bond-forming additives (ii) titration amino groups medium, as well literature dehydrated it concluded by nonaqueous provides them sufficient conformational flexibility needed catalysis.