卡尔斯伯酵母的蛋白水解酶
Proteolytic enzymes of Saccharomyces carlsbergensis.
作者信息
Maddox I S, Hough J S
出版信息
Biochem J. 1970 May;117(5):843-52. doi: 10.1042/bj1170843.
Abstract
- Of four proteolytic enzymes isolated from autolysing Saccharomyces carlsbergensis, one is inactivated at about 45 degrees C, whereas the others are stable at 50 degrees C. pH optima for activity are from 3.0 to 8.0 but maximum stability is between pH6.0 and 6.5. All appear to be glycoproteins, the carbohydrate moiety containing glucose and mannose residues. 2. Lysed protoplasts of the same yeast release four proteolytic enzymes each of which have two pH optima at pH3.0 and 7.0 approximately. Compared with the enzymes from autolysed yeast, resistance to high temperature is much less, and they are not glycoprotein in nature. 3. The same yeast grown with N-acetyltyrosine ethyl ester as nitrogen source secretes into the medium four proteases believed to be glycoprotein in nature. Generally they resemble the enzymes from lysed protoplasts more than those from autolysing yeast.
摘要
- 从自溶的卡尔斯伯酵母中分离出的四种蛋白水解酶中，有一种在约45℃时失活，而其他几种在50℃时稳定。酶活性的最适pH值为3.0至8.0，但最大稳定性在pH6.0至6.5之间。所有这些酶似乎都是糖蛋白，其碳水化合物部分含有葡萄糖和甘露糖残基。2. 同一酵母的裂解原生质体释放出四种蛋白水解酶，每种酶大约在pH3.0和7.0时有两个最适pH值。与自溶酵母中的酶相比，它们对高温的抗性要小得多，并且本质上不是糖蛋白。3. 以N - 乙酰酪氨酸乙酯作为氮源培养的同一酵母向培养基中分泌四种蛋白酶，据信这些蛋白酶本质上是糖蛋白。一般来说，它们与裂解原生质体中的酶更相似，而与自溶酵母中的酶不太相似。
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