{"title":"橄榄毛藻外链1,4- β -葡聚糖酶的纯化及其性质研究。","authors":"A A El-Gindy, R R Saad, E Fawzi","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Exo-1,4-beta-glucanase (E.C. 3.2.1.91) was successively purified by precipitation with acetone, followed by gel filtration on Sephadex G-100 and chromatographed onto DEAE-cellulose. A typical procedure provided 47.14 fold purification with 72.8% yield. The molecular mass of the purified enzyme was found to be 88 kDa by SDS-PAGE. The pH optimum of the enzyme was 5.2 and maximum activity was obtained at 45 degrees C. Km value against alpha-cellulose was 0.65 mg mL(-1). Alpha-cellulose and filter paper were the best substrates for enzyme activity. Enzyme was activated by Mn2+ and Fe3+, inactivated by Cu2+ and completely inhibited by Hg2+ and Ag+.</p>","PeriodicalId":75388,"journal":{"name":"Acta microbiologica Polonica","volume":"52 1","pages":"35-44"},"PeriodicalIF":0.0000,"publicationDate":"2003-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Purification and some properties of exo-1,4-beta-glucanase from Chaetomium olivaceum.\",\"authors\":\"A A El-Gindy, R R Saad, E Fawzi\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Exo-1,4-beta-glucanase (E.C. 3.2.1.91) was successively purified by precipitation with acetone, followed by gel filtration on Sephadex G-100 and chromatographed onto DEAE-cellulose. A typical procedure provided 47.14 fold purification with 72.8% yield. The molecular mass of the purified enzyme was found to be 88 kDa by SDS-PAGE. The pH optimum of the enzyme was 5.2 and maximum activity was obtained at 45 degrees C. Km value against alpha-cellulose was 0.65 mg mL(-1). Alpha-cellulose and filter paper were the best substrates for enzyme activity. Enzyme was activated by Mn2+ and Fe3+, inactivated by Cu2+ and completely inhibited by Hg2+ and Ag+.</p>\",\"PeriodicalId\":75388,\"journal\":{\"name\":\"Acta microbiologica Polonica\",\"volume\":\"52 1\",\"pages\":\"35-44\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2003-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Acta microbiologica Polonica\",\"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 microbiologica Polonica","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Purification and some properties of exo-1,4-beta-glucanase from Chaetomium olivaceum.
Exo-1,4-beta-glucanase (E.C. 3.2.1.91) was successively purified by precipitation with acetone, followed by gel filtration on Sephadex G-100 and chromatographed onto DEAE-cellulose. A typical procedure provided 47.14 fold purification with 72.8% yield. The molecular mass of the purified enzyme was found to be 88 kDa by SDS-PAGE. The pH optimum of the enzyme was 5.2 and maximum activity was obtained at 45 degrees C. Km value against alpha-cellulose was 0.65 mg mL(-1). Alpha-cellulose and filter paper were the best substrates for enzyme activity. Enzyme was activated by Mn2+ and Fe3+, inactivated by Cu2+ and completely inhibited by Hg2+ and Ag+.
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