{"title":"利用分子印迹技术制备表面活性剂包被脂肪酶","authors":"Noriho Kamiya , Masahiro Goto","doi":"10.1016/S0922-338X(97)86774-8","DOIUrl":null,"url":null,"abstract":"<div><p>Modulation of the enantioselectivity of two lipases exhibiting different specificities in the esterification of 2-octanol with lauric acid was investigated by utilizing surfactant-coating and molecular imprinting techniques. The enantioselectivity of the surfactant-coated lipase from <em>Pseudomonas cepacia</em> (PS) was enhanced in the presence of (<em>R</em>)-2-octanol as a print molecule, whereas the enantioselectivity of the lipase from <em>Candida cylindracea</em> (AY) was hardly changed by the imprinting technique. In the case of lipase AY, however, the selectivity of the native enzyme toward the (<em>R</em>)-isomer was changed to a preference for the (<em>S</em>)-isomer as a result of being coating with surfactant molecules. The molecular imprinting effect was prominent in the case of lipase PS, its enantioselectivity in the formation of 2-octanoate in isooctane being enhanced around two-fold compared with that of the native enzyme.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 2","pages":"Pages 237-239"},"PeriodicalIF":0.0000,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0922-338X(97)86774-8","citationCount":"15","resultStr":"{\"title\":\"Preparation of surfactant-coated lipases utilizing the molecular imprinting technique\",\"authors\":\"Noriho Kamiya , Masahiro Goto\",\"doi\":\"10.1016/S0922-338X(97)86774-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Modulation of the enantioselectivity of two lipases exhibiting different specificities in the esterification of 2-octanol with lauric acid was investigated by utilizing surfactant-coating and molecular imprinting techniques. The enantioselectivity of the surfactant-coated lipase from <em>Pseudomonas cepacia</em> (PS) was enhanced in the presence of (<em>R</em>)-2-octanol as a print molecule, whereas the enantioselectivity of the lipase from <em>Candida cylindracea</em> (AY) was hardly changed by the imprinting technique. In the case of lipase AY, however, the selectivity of the native enzyme toward the (<em>R</em>)-isomer was changed to a preference for the (<em>S</em>)-isomer as a result of being coating with surfactant molecules. The molecular imprinting effect was prominent in the case of lipase PS, its enantioselectivity in the formation of 2-octanoate in isooctane being enhanced around two-fold compared with that of the native enzyme.</p></div>\",\"PeriodicalId\":15696,\"journal\":{\"name\":\"Journal of Fermentation and Bioengineering\",\"volume\":\"85 2\",\"pages\":\"Pages 237-239\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0922-338X(97)86774-8\",\"citationCount\":\"15\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Fermentation and Bioengineering\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0922338X97867748\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Fermentation and Bioengineering","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0922338X97867748","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Preparation of surfactant-coated lipases utilizing the molecular imprinting technique
Modulation of the enantioselectivity of two lipases exhibiting different specificities in the esterification of 2-octanol with lauric acid was investigated by utilizing surfactant-coating and molecular imprinting techniques. The enantioselectivity of the surfactant-coated lipase from Pseudomonas cepacia (PS) was enhanced in the presence of (R)-2-octanol as a print molecule, whereas the enantioselectivity of the lipase from Candida cylindracea (AY) was hardly changed by the imprinting technique. In the case of lipase AY, however, the selectivity of the native enzyme toward the (R)-isomer was changed to a preference for the (S)-isomer as a result of being coating with surfactant molecules. The molecular imprinting effect was prominent in the case of lipase PS, its enantioselectivity in the formation of 2-octanoate in isooctane being enhanced around two-fold compared with that of the native enzyme.