{"title":"Studies on rifamycin oxidase immobilized on kappa-carrageenan gel.","authors":"U C Banerjee","doi":"10.3109/10731199309117391","DOIUrl":null,"url":null,"abstract":"<p><p>Rifamycin oxidase from Curvularia lunata var. aeria was immobilized on kappa-carrageenan gel where the enzyme showed excellent catalyzing activity and operational stability. Factors affecting the activity of immobilized enzyme preparation such as pH and temperature were investigated. Thermostability of the immobilized enzyme preparation was checked at 30 and 40 degrees C and it was found that the thermostability of the immobilized rifamycin oxidase activity has increased compared to free enzyme. Transformation of rifamycin B to rifamycin S was also carried out with the immobilized enzyme preparation. Kappa-carrageenan immobilized rifamycin oxidase was also reused several times for the transformation of rifamycin B to rifamycin S.</p>","PeriodicalId":77039,"journal":{"name":"Biomaterials, artificial cells, and immobilization biotechnology : official journal of the International Society for Artificial Cells and Immobilization Biotechnology","volume":"21 5","pages":"665-74"},"PeriodicalIF":0.0000,"publicationDate":"1993-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199309117391","citationCount":"2","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biomaterials, artificial cells, and immobilization biotechnology : official journal of the International Society for Artificial Cells and Immobilization Biotechnology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3109/10731199309117391","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 2
Abstract
Rifamycin oxidase from Curvularia lunata var. aeria was immobilized on kappa-carrageenan gel where the enzyme showed excellent catalyzing activity and operational stability. Factors affecting the activity of immobilized enzyme preparation such as pH and temperature were investigated. Thermostability of the immobilized enzyme preparation was checked at 30 and 40 degrees C and it was found that the thermostability of the immobilized rifamycin oxidase activity has increased compared to free enzyme. Transformation of rifamycin B to rifamycin S was also carried out with the immobilized enzyme preparation. Kappa-carrageenan immobilized rifamycin oxidase was also reused several times for the transformation of rifamycin B to rifamycin S.
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