{"title":"微生物转谷氨酰胺酶对酪蛋白酸钠的交联作用。","authors":"P C Lorenzen, E Schlimme, N Roos","doi":"10.1002/(sici)1521-3803(199808)42:03/04<151::aid-food151>3.3.co;2-5","DOIUrl":null,"url":null,"abstract":"<p><p>Sodium caseinate is an effective substrate for transglutaminase. Crosslinking takes place at fast reaction rates resulting in high degrees of crosslinking. The polymers can be hydrolysed by trypsin, but the proteolysates contain residual portions of non- or partlyhydrolysed aggregates. Crosslinking of hydrolysed sodium caseinate decreased the number of free amino groups, but leads only to a very small increase in molecular weight of the peptides.</p>","PeriodicalId":11281,"journal":{"name":"Die Nahrung","volume":"42 3-4","pages":"151-4"},"PeriodicalIF":0.0000,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"57","resultStr":"{\"title\":\"Crosslinking of sodium caseinate by a microbial transglutaminase.\",\"authors\":\"P C Lorenzen, E Schlimme, N Roos\",\"doi\":\"10.1002/(sici)1521-3803(199808)42:03/04<151::aid-food151>3.3.co;2-5\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Sodium caseinate is an effective substrate for transglutaminase. Crosslinking takes place at fast reaction rates resulting in high degrees of crosslinking. The polymers can be hydrolysed by trypsin, but the proteolysates contain residual portions of non- or partlyhydrolysed aggregates. Crosslinking of hydrolysed sodium caseinate decreased the number of free amino groups, but leads only to a very small increase in molecular weight of the peptides.</p>\",\"PeriodicalId\":11281,\"journal\":{\"name\":\"Die Nahrung\",\"volume\":\"42 3-4\",\"pages\":\"151-4\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"57\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Die Nahrung\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1002/(sici)1521-3803(199808)42:03/04<151::aid-food151>3.3.co;2-5\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Die Nahrung","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1002/(sici)1521-3803(199808)42:03/04<151::aid-food151>3.3.co;2-5","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Crosslinking of sodium caseinate by a microbial transglutaminase.
Sodium caseinate is an effective substrate for transglutaminase. Crosslinking takes place at fast reaction rates resulting in high degrees of crosslinking. The polymers can be hydrolysed by trypsin, but the proteolysates contain residual portions of non- or partlyhydrolysed aggregates. Crosslinking of hydrolysed sodium caseinate decreased the number of free amino groups, but leads only to a very small increase in molecular weight of the peptides.
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