从扇贝废料中回收溶菌酶。

B Myrnes, A Johansen
{"title":"从扇贝废料中回收溶菌酶。","authors":"B Myrnes,&nbsp;A Johansen","doi":"10.1080/10826069408010083","DOIUrl":null,"url":null,"abstract":"<p><p>A crude lysozyme preparation was recovered in waste from the scallop processing industry. Lysozyme was then purified 229-fold in preparative scale by chromatography on S Sepharose and Blue Sepharose. Further purification on Sephacryl S-200 resulted in a lysozyme preparation with a specific activity of 64,000 units/mg protein. The apparent molecular mass of the partially purified lysozyme was 10 kDa as judged by gel filtration. Optimum pH for lysis of Micrococus luteus under the present conditions was 5.2. The enzyme was very active at low temperatures. At 4 degrees C the scallop viscera lysozyme exhibits about 55% of the activity measured at 37 degrees C.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"24 1","pages":"69-80"},"PeriodicalIF":0.0000,"publicationDate":"1994-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069408010083","citationCount":"31","resultStr":"{\"title\":\"Recovery of lysozyme from scallop waste.\",\"authors\":\"B Myrnes,&nbsp;A Johansen\",\"doi\":\"10.1080/10826069408010083\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>A crude lysozyme preparation was recovered in waste from the scallop processing industry. Lysozyme was then purified 229-fold in preparative scale by chromatography on S Sepharose and Blue Sepharose. Further purification on Sephacryl S-200 resulted in a lysozyme preparation with a specific activity of 64,000 units/mg protein. The apparent molecular mass of the partially purified lysozyme was 10 kDa as judged by gel filtration. Optimum pH for lysis of Micrococus luteus under the present conditions was 5.2. The enzyme was very active at low temperatures. At 4 degrees C the scallop viscera lysozyme exhibits about 55% of the activity measured at 37 degrees C.</p>\",\"PeriodicalId\":20391,\"journal\":{\"name\":\"Preparative biochemistry\",\"volume\":\"24 1\",\"pages\":\"69-80\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-02-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1080/10826069408010083\",\"citationCount\":\"31\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Preparative biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1080/10826069408010083\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Preparative biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/10826069408010083","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 31

摘要

从扇贝加工工业的废液中回收了一种粗溶菌酶制剂。通过S Sepharose和Blue Sepharose的层析,在制备尺度上纯化了229倍的溶菌酶。进一步对Sephacryl S-200进行纯化,得到比活性为64,000单位/mg蛋白的溶菌酶。经凝胶过滤,部分纯化的溶菌酶表观分子质量为10 kDa。在本实验条件下,酵解黄微球菌的最佳pH为5.2。这种酶在低温下非常活跃。在4℃时,扇贝内脏溶菌酶的活性约为37℃时的55%。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Recovery of lysozyme from scallop waste.

A crude lysozyme preparation was recovered in waste from the scallop processing industry. Lysozyme was then purified 229-fold in preparative scale by chromatography on S Sepharose and Blue Sepharose. Further purification on Sephacryl S-200 resulted in a lysozyme preparation with a specific activity of 64,000 units/mg protein. The apparent molecular mass of the partially purified lysozyme was 10 kDa as judged by gel filtration. Optimum pH for lysis of Micrococus luteus under the present conditions was 5.2. The enzyme was very active at low temperatures. At 4 degrees C the scallop viscera lysozyme exhibits about 55% of the activity measured at 37 degrees C.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信