PRODUCTION, DISTRIBUTION, AND KINETIC-PROPERTIES OF INULINASE IN CONTINUOUS CULTURES OF KLUYVEROMYCES-MARXIANUS CBS-6556
PRODUCTION, DISTRIBUTION, AND KINETIC-PROPERTIES OF INULINASE IN CONTINUOUS CULTURES OF KLUYVEROMYCES-MARXIANUS CBS-6556
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DOI：
10.1128/aem.54.5.1131-1137.1988
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发表时间：
1988-05-01
影响因子：
4.4
通讯作者：
VANDIJKEN, JP
中科院分区：
文献类型：
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作者：
ROUWENHORST, RJ;VISSER, LE;VANDIJKEN, JP
从几种克鲁维酵母属菌株的筛选中，选择酵母马克斯克鲁维酵母CBS 6556用于研究与菊粉酶的商业生产相关的参数（EC 3.2.1.7）。该酵母在高温（40 - 45 ℃）下的生长、底物特异性和菊粉酶生产方面表现出优良的上级特性。在蔗糖限制恒化培养生长在矿物培养基中，酶的量从52 U毫克细胞干重-1在D = 0.8 h-1。氮限制培养物的实验进一步证实，酶的合成受培养物中残余糖浓度的负控制。在非糖底物上生长期间观察到高酶活性，表明酶的合成是解阻遏/阻遏机制的结果。K.马克思主义与细胞壁有关。这种酶可以通过对细胞进行简单的化学处理从细胞壁中释放出来。结果上的酶的分布上的培养条件的影响。菊粉酶与蔗糖，棉子糖，水苏糖，菊粉作为底物的活性和表现出的S/I比（与蔗糖和菊粉的相对活性）为15在标准测定条件下。随着底物链长的增加，酶活性降低。
From a screening of several Kluyveromyces strains, the yeast Kluyveromyces marxianus CBS 6556 was selected for a study of the parameters relevant to the commercial production of inulinase (EC 3.2.1.7). This yeast exhibited superior properties with respect to growth at elevated temperatures (40 to 45.degree.C), substrate specificity, and inulinase production. In sucrose-limited chemostat cultures growing on mineral medium, the amount of enzyme decreased from 52 U mg of cell dry weight-1 at D = 0.8 h-1. Experiments with nitrogen-limited cultures further confirmed that synthesis of the enzyme is negatively controlled by the residual sugar concentration in the culture. High enzyme activities were observed during growth on nonsugar substrates, indicating that synthesis of the enzyme is a result of a derepression/repression mechanism. A substantial part of the inulinase produced by K. marxianus was associated with the cell wall. The enzyme could be released from the cell wall via a simple chemical treatment of cells. Results are presented on the effect of cultivation conditions on the distribution of the enzyme. Inulinase was active with sucrose, raffinose, stachyose, and inulin as substrates and exhibited an S/I ratio (relative activities with sucrose and inulin) of 15 under standard assay conditions. The enzyme activity decreased with increasing chain length of the substrate.