Sudovtsov V E
Prikl Biokhim Mikrobiol. 1991 Jan-Feb;27(1):61-7.
The author studied the activity of alcohol dehydrogenase from the cytoplasm of Saccharomyces cerevisiae, Saccharomyces carlsbergensis, Candida utilis and Torulopsis candida cells. The "classical" alcohol dehydrogenase and the octanol dehydrogenase from the T. candida cytoplasm are active in a wide range of pH from 7.0 to 10.5, whereas in the cytoplasm of other yeast cells these enzymes are active in a relatively narrow range of pH. Essential differences were also revealed in the co-enzyme used. In the cytoplasm of S. carlsbergensis and T. candida cells the enzymes display the activity only in the presence of NAD+, while in the other cells, in the presence of both NAD+ and NADP+. The substrate specificity varies as well. While the general activity of alcohol dehydrogenases from the T. candida cytoplasm decreases gradually with the growth of the alcohol radical from C2 to C10, a different regularity is observed in the other cells. Optimal conditions were chosen for maintaining the enzyme activity during prolonged storage of cytoplasm preparations from the yeasts under study.
作者研究了酿酒酵母、卡尔斯伯酵母、产朊假丝酵母和假丝酵母细胞胞质中乙醇脱氢酶的活性。“经典”乙醇脱氢酶和假丝酵母胞质中的辛醇脱氢酶在pH值7.0至10.5的较宽范围内具有活性,而在其他酵母细胞的胞质中,这些酶在相对较窄的pH范围内具有活性。在辅酶的使用上也发现了本质差异。在卡尔斯伯酵母和假丝酵母细胞的胞质中,这些酶仅在存在NAD+时才表现出活性,而在其他细胞中,则在同时存在NAD+和NADP+时表现出活性。底物特异性也有所不同。虽然假丝酵母胞质中乙醇脱氢酶的总体活性随着醇基从C2增长到C10而逐渐降低,但在其他细胞中观察到不同的规律。选择了最佳条件,以在长时间储存所研究酵母的胞质制剂期间保持酶活性。