巴厘岛Banyuwedang产蛋白酶菌的鉴定及其蛋白酶的性质

Q3 Environmental Science
D. S. Zilda, Y. N. Fawzya, A. Uria
{"title":"巴厘岛Banyuwedang产蛋白酶菌的鉴定及其蛋白酶的性质","authors":"D. S. Zilda, Y. N. Fawzya, A. Uria","doi":"10.15578/SQUALEN.V13I3.367","DOIUrl":null,"url":null,"abstract":"Proteases or peptidases is known as a largest group of hydrolytic enzymes and have been applied in various industries such as food, pharmacy, leather, detergent and waste treatment. Although they are also produced by plants and animals, microbes remain the main source of proteases in the world market which mostly derived from Bacillus sp. Aims of this research were to identify isolate BII-1 and study its protease. Analysis of 16Sr RNA sequencing showed the identity of BII-1 as Bacillus subtilis (99% similarity with the same species in GenBank). It was found that protease from BII-1 exhibited optimal temperature and pH of 50 oC and 8-9, respectively. It was activated by Li2+, Na2+, Mg2+ and K+. The degenerated primer for protease gene was designed, and a partial protease gene was amplified from BII-1. The sequencing result showed that this amplified gene shared 100 and 99% similarity with those from Geobacillus thermophiles and Bacillus subtilis in the GenBank, respectively.Keywords: protease, bacteria, Bacillus subtilis, Geobacillus thermophylus","PeriodicalId":21935,"journal":{"name":"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology","volume":"62 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2018-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"4","resultStr":"{\"title\":\"Identification of Protease-Producing Bacteria Isolated from Banyuwedang, Bali, and Characterization of its Protease\",\"authors\":\"D. S. Zilda, Y. N. Fawzya, A. Uria\",\"doi\":\"10.15578/SQUALEN.V13I3.367\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Proteases or peptidases is known as a largest group of hydrolytic enzymes and have been applied in various industries such as food, pharmacy, leather, detergent and waste treatment. Although they are also produced by plants and animals, microbes remain the main source of proteases in the world market which mostly derived from Bacillus sp. Aims of this research were to identify isolate BII-1 and study its protease. Analysis of 16Sr RNA sequencing showed the identity of BII-1 as Bacillus subtilis (99% similarity with the same species in GenBank). It was found that protease from BII-1 exhibited optimal temperature and pH of 50 oC and 8-9, respectively. It was activated by Li2+, Na2+, Mg2+ and K+. The degenerated primer for protease gene was designed, and a partial protease gene was amplified from BII-1. The sequencing result showed that this amplified gene shared 100 and 99% similarity with those from Geobacillus thermophiles and Bacillus subtilis in the GenBank, respectively.Keywords: protease, bacteria, Bacillus subtilis, Geobacillus thermophylus\",\"PeriodicalId\":21935,\"journal\":{\"name\":\"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology\",\"volume\":\"62 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2018-12-30\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"4\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.15578/SQUALEN.V13I3.367\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"Environmental Science\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.15578/SQUALEN.V13I3.367","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"Environmental Science","Score":null,"Total":0}
引用次数: 4

摘要

蛋白酶或肽酶被称为最大的水解酶群,在食品、制药、皮革、洗涤剂和废物处理等各个行业都有应用。虽然它们也可以由植物和动物产生,但在世界市场上,微生物仍然是蛋白酶的主要来源,主要来源于芽孢杆菌。本研究的目的是鉴定分离物BII-1并对其蛋白酶进行研究。16Sr RNA测序结果显示,BII-1为枯草芽孢杆菌(Bacillus subtilis),与GenBank同源菌株相似性达99%。结果表明,BII-1蛋白酶的最适温度和pH分别为50℃和8-9℃。它被Li2+、Na2+、Mg2+和K+激活。设计了蛋白酶基因的退化引物,并从BII-1中扩增出部分蛋白酶基因。测序结果表明,该扩增基因与GenBank中嗜热地杆菌和枯草芽孢杆菌基因的相似性分别为100%和99%。关键词:蛋白酶;细菌;枯草芽孢杆菌
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Identification of Protease-Producing Bacteria Isolated from Banyuwedang, Bali, and Characterization of its Protease
Proteases or peptidases is known as a largest group of hydrolytic enzymes and have been applied in various industries such as food, pharmacy, leather, detergent and waste treatment. Although they are also produced by plants and animals, microbes remain the main source of proteases in the world market which mostly derived from Bacillus sp. Aims of this research were to identify isolate BII-1 and study its protease. Analysis of 16Sr RNA sequencing showed the identity of BII-1 as Bacillus subtilis (99% similarity with the same species in GenBank). It was found that protease from BII-1 exhibited optimal temperature and pH of 50 oC and 8-9, respectively. It was activated by Li2+, Na2+, Mg2+ and K+. The degenerated primer for protease gene was designed, and a partial protease gene was amplified from BII-1. The sequencing result showed that this amplified gene shared 100 and 99% similarity with those from Geobacillus thermophiles and Bacillus subtilis in the GenBank, respectively.Keywords: protease, bacteria, Bacillus subtilis, Geobacillus thermophylus
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
CiteScore
1.40
自引率
0.00%
发文量
10
审稿时长
16 weeks
×
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