{"title":"海藻酸盐沉淀法一步纯化花生磷脂酶D。","authors":"S Sharma, A Sharma, M N Gupta","doi":"10.1023/a:1008121005974","DOIUrl":null,"url":null,"abstract":"<p><p>A simple titrimetric assay with soybean lecithin has been used for screening phospholipase D activity from some plant sources, viz. peanut, wheat germ, cabbage and carrot. The enzyme from peanut has been purified by binding to alginate which is a water soluble polymer. The purification consisted of co-precipitation of enzyme with alginate upon addition of 0.06 M Ca++. The enzyme was eluted from the polymer using 0.2 M sodium chloride. The activity recovery was 61% with 34 fold purification.</p>","PeriodicalId":9179,"journal":{"name":"Bioseparation","volume":"9 2","pages":"93-8"},"PeriodicalIF":0.0000,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1023/a:1008121005974","citationCount":"21","resultStr":"{\"title\":\"One step purification of peanut phospholipase D by precipitation with alginate.\",\"authors\":\"S Sharma, A Sharma, M N Gupta\",\"doi\":\"10.1023/a:1008121005974\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>A simple titrimetric assay with soybean lecithin has been used for screening phospholipase D activity from some plant sources, viz. peanut, wheat germ, cabbage and carrot. The enzyme from peanut has been purified by binding to alginate which is a water soluble polymer. The purification consisted of co-precipitation of enzyme with alginate upon addition of 0.06 M Ca++. The enzyme was eluted from the polymer using 0.2 M sodium chloride. The activity recovery was 61% with 34 fold purification.</p>\",\"PeriodicalId\":9179,\"journal\":{\"name\":\"Bioseparation\",\"volume\":\"9 2\",\"pages\":\"93-8\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2000-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1023/a:1008121005974\",\"citationCount\":\"21\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bioseparation\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1023/a:1008121005974\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioseparation","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1023/a:1008121005974","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 21
摘要
大豆卵磷脂的简单滴定法已被用于筛选一些植物来源的磷脂酶D活性，如花生、小麦胚芽、卷心菜和胡萝卜。通过与海藻酸盐(一种水溶性聚合物)结合纯化花生酶。纯化是在添加0.06 M Ca++的情况下，酶与海藻酸盐共沉淀。用0.2 M氯化钠从聚合物中洗脱酶。经34倍纯化，活性回收率为61%。
One step purification of peanut phospholipase D by precipitation with alginate.
A simple titrimetric assay with soybean lecithin has been used for screening phospholipase D activity from some plant sources, viz. peanut, wheat germ, cabbage and carrot. The enzyme from peanut has been purified by binding to alginate which is a water soluble polymer. The purification consisted of co-precipitation of enzyme with alginate upon addition of 0.06 M Ca++. The enzyme was eluted from the polymer using 0.2 M sodium chloride. The activity recovery was 61% with 34 fold purification.
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