乳酸乳球菌IO-1产生的肽抗生素Nisin Z的一些特性

H. Matsusaki, K. Sonomoto, A. Ishizaki
{"title":"乳酸乳球菌IO-1产生的肽抗生素Nisin Z的一些特性","authors":"H. Matsusaki, K. Sonomoto, A. Ishizaki","doi":"10.3136/FSTI9596T9798.4.290","DOIUrl":null,"url":null,"abstract":"Lactococcus lactis IO-1 isolated in our laboratory produces a peptide antibiotic, a natural nisin variant, nisin Z. Nisin Z was heat stable at acidic pH and showed a bactericidal mode of action against an indicator strain, Bacillus subtilis C1. The effect of proteolytic enzyme treatment on the activity and the antimicrobial spectrum were tested. These results indicated nearly the same characteristics as those of nisin A. In this study, it was found that two nisin variants (nisin Z and nisin A) were practically inactivated by proteinase K and actinase E. Interestingly, nisin-producing strains, L. lactis IO-1 and L. lactis NCDO 497 (a nisin A producer) were sensitive to a high concentration of nisin variants including their own products. The growth of a Gram-negative bacterium, Escherichia coli, was also inhibited by a high concentration of nisin, although nisin producers and Gram-negative bacteria are generally resistant to nisin variants.","PeriodicalId":12457,"journal":{"name":"Food Science and Technology International, Tokyo","volume":"16 1","pages":"290-294"},"PeriodicalIF":0.0000,"publicationDate":"1998-11-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"23","resultStr":"{\"title\":\"Some Characteristics of Nisin Z, a Peptide Antibiotic Produced by Lactococcus lactis IO-1\",\"authors\":\"H. Matsusaki, K. Sonomoto, A. Ishizaki\",\"doi\":\"10.3136/FSTI9596T9798.4.290\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Lactococcus lactis IO-1 isolated in our laboratory produces a peptide antibiotic, a natural nisin variant, nisin Z. Nisin Z was heat stable at acidic pH and showed a bactericidal mode of action against an indicator strain, Bacillus subtilis C1. The effect of proteolytic enzyme treatment on the activity and the antimicrobial spectrum were tested. These results indicated nearly the same characteristics as those of nisin A. In this study, it was found that two nisin variants (nisin Z and nisin A) were practically inactivated by proteinase K and actinase E. Interestingly, nisin-producing strains, L. lactis IO-1 and L. lactis NCDO 497 (a nisin A producer) were sensitive to a high concentration of nisin variants including their own products. The growth of a Gram-negative bacterium, Escherichia coli, was also inhibited by a high concentration of nisin, although nisin producers and Gram-negative bacteria are generally resistant to nisin variants.\",\"PeriodicalId\":12457,\"journal\":{\"name\":\"Food Science and Technology International, Tokyo\",\"volume\":\"16 1\",\"pages\":\"290-294\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-11-25\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"23\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Science and Technology International, Tokyo\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3136/FSTI9596T9798.4.290\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Science and Technology International, Tokyo","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3136/FSTI9596T9798.4.290","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 23

摘要

我们实验室分离的乳酸乳球菌IO-1产生一种肽抗生素,一种天然的nisin变种,nisin Z。nisin Z在酸性pH下热稳定,并对指示菌株枯草芽孢杆菌C1表现出杀菌模式。考察了蛋白水解酶处理对其活性和抑菌谱的影响。这些结果显示了与nisin A几乎相同的特性。在本研究中,我们发现两种nisin变体(nisin Z和nisin A)实际上被蛋白酶K和actinase e灭活。有趣的是,nisin产生菌株L. lactis IO-1和L. lactis NCDO 497(一种nisin A产生菌株)对包括其自身产物在内的高浓度nisin变体敏感。一种革兰氏阴性菌——大肠杆菌的生长也被高浓度的乳酸链球菌素抑制,尽管乳酸链球菌素的产生菌和革兰氏阴性菌通常对乳酸链球菌素变种具有耐药性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Some Characteristics of Nisin Z, a Peptide Antibiotic Produced by Lactococcus lactis IO-1
Lactococcus lactis IO-1 isolated in our laboratory produces a peptide antibiotic, a natural nisin variant, nisin Z. Nisin Z was heat stable at acidic pH and showed a bactericidal mode of action against an indicator strain, Bacillus subtilis C1. The effect of proteolytic enzyme treatment on the activity and the antimicrobial spectrum were tested. These results indicated nearly the same characteristics as those of nisin A. In this study, it was found that two nisin variants (nisin Z and nisin A) were practically inactivated by proteinase K and actinase E. Interestingly, nisin-producing strains, L. lactis IO-1 and L. lactis NCDO 497 (a nisin A producer) were sensitive to a high concentration of nisin variants including their own products. The growth of a Gram-negative bacterium, Escherichia coli, was also inhibited by a high concentration of nisin, although nisin producers and Gram-negative bacteria are generally resistant to nisin variants.
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:481959085
Book学术官方微信