Franke-Rinker D, Behrens U, Nöckel E
Z Allg Mikrobiol. 1983;23(2):75-80. doi: 10.1002/jobm.3630230202.
The connection between the kinetics of citrate-isocitrate overproduction by Saccharomycopsis lipolytica in glucose media and the specific activities of the enzymes being related to overproduction has been investigated. The specific activities of citrate synthase, aconitate hydratase, NAD+-linked and NADP+-linked isocitrate dehydrogenase decline significantly after exhaustion of the nitrogen source, whereas the activity of the pyruvate carboxylase remains relatively constant and corresponds to changes of the production rate. The results are compared with those obtained by fermentations in n-alkane media and discussed in relation to mechanisms of overproduction.
研究了解脂耶氏酵母在葡萄糖培养基中柠檬酸-异柠檬酸过量生产的动力学与过量生产相关酶的比活性之间的联系。氮源耗尽后,柠檬酸合酶、乌头酸水合酶、NAD⁺连接和NADP⁺连接的异柠檬酸脱氢酶的比活性显著下降,而丙酮酸羧化酶的活性保持相对恒定,并与生产率的变化相对应。将结果与在正构烷烃培养基中发酵获得的结果进行比较,并就过量生产的机制进行了讨论。