{"title":"荧光假单胞菌脂肪酶在无溶剂条件下催化牛油脂肪的酯化反应","authors":"P. Kalo, H. Huotari, M. Antila","doi":"10.1002/LIPI.19890910706","DOIUrl":null,"url":null,"abstract":"Butter fat was interesterified in a medium of low water content in the absence of a solvent with P. fluorescens lipase as catalyst at various temperatures. In the reaction products of interesterifications at 50 o C and 60 o C, the TAG compositions determined by GLC, and the FA compositions at the sn-2 position determined by enzymatic deacylation, were close to random, indicating the positional non-specificity of P. fluorescens lipase under the reaction conditions used","PeriodicalId":18590,"journal":{"name":"Milchwissenschaft-milk Science International","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"54","resultStr":"{\"title\":\"Pseudomonas fluorescens lipase-catalysed interesterification of butter fat in the absence of a solvent\",\"authors\":\"P. Kalo, H. Huotari, M. Antila\",\"doi\":\"10.1002/LIPI.19890910706\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Butter fat was interesterified in a medium of low water content in the absence of a solvent with P. fluorescens lipase as catalyst at various temperatures. In the reaction products of interesterifications at 50 o C and 60 o C, the TAG compositions determined by GLC, and the FA compositions at the sn-2 position determined by enzymatic deacylation, were close to random, indicating the positional non-specificity of P. fluorescens lipase under the reaction conditions used\",\"PeriodicalId\":18590,\"journal\":{\"name\":\"Milchwissenschaft-milk Science International\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1900-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"54\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Milchwissenschaft-milk Science International\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1002/LIPI.19890910706\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Milchwissenschaft-milk Science International","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1002/LIPI.19890910706","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Pseudomonas fluorescens lipase-catalysed interesterification of butter fat in the absence of a solvent
Butter fat was interesterified in a medium of low water content in the absence of a solvent with P. fluorescens lipase as catalyst at various temperatures. In the reaction products of interesterifications at 50 o C and 60 o C, the TAG compositions determined by GLC, and the FA compositions at the sn-2 position determined by enzymatic deacylation, were close to random, indicating the positional non-specificity of P. fluorescens lipase under the reaction conditions used