Trehalases from the ascospores of Neurospora tetrasperma and the mycelium of N. crassa were compared. Enzymes from both sources have identical electrophoretic mobilities, Km's, responses to pH, immunological reactions, and activities in low-molarity buffers. Because both enzymes are so similar, conclusions about the properties of the ascospore enzyme may, be made by studying mycelial trehalase. Mycelial trehalase is most active and stable in low-molarity buffers. The enzyme exists in at least three species; the smallest has a molecular weight between 105,000 and 125,000 and is predominant in low-molarity buffers at 37 C. The stability of trehalase to heating at 65 C can be increased by increasing enzyme concentration and by the addition of polyols. Ascospores contain large amounts of trehalose, which protects trehalase from heat inactivation at 65 C. The importance of this phenomenon in vivo and its relationship to the localization of trehalase in ascospores is discussed.
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机译：来自四孢神经孢子的子囊孢子和 N菌丝体的海藻糖酶。比较了crassa 。两种来源的酶具有相同的电泳迁移率， K m ，对pH的响应，免疫反应以及低分子缓冲液中的活性。因为这两种酶是如此相似，所以可以通过研究菌丝体海藻糖酶来得出有关子囊孢子酶特性的结论。菌丝体海藻糖酶在低分子量缓冲液中最活跃，最稳定。该酶至少存在三种。最小的分子量在105,000和125,000之间，主要在37°C的低分子缓冲液中。通过增加酶的浓度和添加多元醇，可以提高海藻糖酶在65°C加热的稳定性。子囊孢子含有大量的海藻糖，可保护海藻糖酶在65℃下免于热失活。讨论了该现象在体内的重要性及其与子囊孢子中海藻糖酶定位的关系。
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