{"title":"[相关蛋白酶对失活α -淀粉酶的降解]。","authors":"R Ulbrich, G Kvesitadze, A Schellenberger","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Alpha-Amylase preparations often contain small quantities of proteolytic activity which are difficult to remove. On the example of fungal alpha-amylase, such associated proteases have been shown to possess a specific activity to the denatured amylase molecules. The amylase is not attacked under native conditions, whereas in the thermal denaturation a rapid degradation of only the inactivated molecules occurs. A specific metabolic function of these associated proteases in the return of denatured amylase molecules to the amino acid pool is suggested.</p>","PeriodicalId":6985,"journal":{"name":"Acta biologica et medica Germanica","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Degradation of inactivated alpha-amylase by associated proteases].\",\"authors\":\"R Ulbrich, G Kvesitadze, A Schellenberger\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Alpha-Amylase preparations often contain small quantities of proteolytic activity which are difficult to remove. On the example of fungal alpha-amylase, such associated proteases have been shown to possess a specific activity to the denatured amylase molecules. The amylase is not attacked under native conditions, whereas in the thermal denaturation a rapid degradation of only the inactivated molecules occurs. A specific metabolic function of these associated proteases in the return of denatured amylase molecules to the amino acid pool is suggested.</p>\",\"PeriodicalId\":6985,\"journal\":{\"name\":\"Acta biologica et medica Germanica\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1982-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Acta biologica et medica Germanica\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta biologica et medica Germanica","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[Degradation of inactivated alpha-amylase by associated proteases].
Alpha-Amylase preparations often contain small quantities of proteolytic activity which are difficult to remove. On the example of fungal alpha-amylase, such associated proteases have been shown to possess a specific activity to the denatured amylase molecules. The amylase is not attacked under native conditions, whereas in the thermal denaturation a rapid degradation of only the inactivated molecules occurs. A specific metabolic function of these associated proteases in the return of denatured amylase molecules to the amino acid pool is suggested.