{"title":"放线菌α -半乳糖苷酶同工酶的纯化及性质研究。","authors":"Monika Prendecka, Krystyna Szyjka, Jerzy Rogalski","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Phlebia radiata formed extracellular alpha-galactosidase when it was grown in a culture containing wheat bran or locus bean gum as a carbon source. Their activities were optimal at pH 5.0, and demonstrated the highest level of activity at 60 degrees C. Highly purified isoforms of alpha-galactosidase (AGaS-m1, AGaS-m2, AGaS-m3) isolated from the media with galactomannan and (AGaS-b1, AGaS-b2, AGaS-b3) from the media with wheat bran were obtained by means of the column chromatography on Q-Sepharose and chromatofosussing on Polybuffer Exchanger PBE-94.</p>","PeriodicalId":75388,"journal":{"name":"Acta microbiologica Polonica","volume":"52 1","pages":"25-33"},"PeriodicalIF":0.0000,"publicationDate":"2003-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Purification and properties of alpha-galactosidase isosymes from Phlebia radiata.\",\"authors\":\"Monika Prendecka, Krystyna Szyjka, Jerzy Rogalski\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Phlebia radiata formed extracellular alpha-galactosidase when it was grown in a culture containing wheat bran or locus bean gum as a carbon source. Their activities were optimal at pH 5.0, and demonstrated the highest level of activity at 60 degrees C. Highly purified isoforms of alpha-galactosidase (AGaS-m1, AGaS-m2, AGaS-m3) isolated from the media with galactomannan and (AGaS-b1, AGaS-b2, AGaS-b3) from the media with wheat bran were obtained by means of the column chromatography on Q-Sepharose and chromatofosussing on Polybuffer Exchanger PBE-94.</p>\",\"PeriodicalId\":75388,\"journal\":{\"name\":\"Acta microbiologica Polonica\",\"volume\":\"52 1\",\"pages\":\"25-33\"},\"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 properties of alpha-galactosidase isosymes from Phlebia radiata.
Phlebia radiata formed extracellular alpha-galactosidase when it was grown in a culture containing wheat bran or locus bean gum as a carbon source. Their activities were optimal at pH 5.0, and demonstrated the highest level of activity at 60 degrees C. Highly purified isoforms of alpha-galactosidase (AGaS-m1, AGaS-m2, AGaS-m3) isolated from the media with galactomannan and (AGaS-b1, AGaS-b2, AGaS-b3) from the media with wheat bran were obtained by means of the column chromatography on Q-Sepharose and chromatofosussing on Polybuffer Exchanger PBE-94.