枯草芽孢杆菌 BSP 菌株的一种恒温蛋白酶的特性。

IF 3.5 3区 生物学 Q2 BIOTECHNOLOGY & APPLIED MICROBIOLOGY BMC Biotechnology Pub Date : 2024-07-15 DOI:10.1186/s12896-024-00870-5
Tanveer Majeed, Charles C Lee, William J Orts, Romana Tabassum, Tawaf Ali Shah, Yousef A Bin Jardan, Turki M Dawoud, Mohammed Bourhia
{"title":"枯草芽孢杆菌 BSP 菌株的一种恒温蛋白酶的特性。","authors":"Tanveer Majeed, Charles C Lee, William J Orts, Romana Tabassum, Tawaf Ali Shah, Yousef A Bin Jardan, Turki M Dawoud, Mohammed Bourhia","doi":"10.1186/s12896-024-00870-5","DOIUrl":null,"url":null,"abstract":"<p><p>This study used conservative one variable-at-a-time study and statistical surface response methods to increase the yields of an extracellular thermostable protease secreted by a newly identified thermophilic Bacillus subtilis BSP strain. Using conventional optimization techniques, physical parameters in submerged fermentation were adjusted at the shake flask level to reach 184 U/mL. These physicochemical parameters were further optimized by statistical surface response methodology using Box Behnken design, and the protease yield increased to 295 U/mL. The protease was purified and characterized biochemically. Both Ca<sup>2+</sup> and Fe<sup>2+</sup> increased the activity of the 36 kDa protease enzyme. Based on its strong inhibition by ethylenediaminetetracetate (EDTA), the enzyme was confirmed to be a metalloprotease. The protease was also resistant to various organic solvents (benzene, ethanol, methanol), surfactants (Triton X-100), sodium dodecyl sulfate (SDS), Tween 20, Tween-80 and oxidants hydrogen per oxide (H<sub>2</sub>O<sub>2</sub>). Characteristics, such as tolerance to high SDS and H<sub>2</sub>O<sub>2</sub> concentrations, indicate that this protease has potential applications in the pharmaceutical and detergent industries.</p>","PeriodicalId":8905,"journal":{"name":"BMC Biotechnology","volume":null,"pages":null},"PeriodicalIF":3.5000,"publicationDate":"2024-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11247832/pdf/","citationCount":"0","resultStr":"{\"title\":\"Characterization of a thermostable protease from Bacillus subtilis BSP strain.\",\"authors\":\"Tanveer Majeed, Charles C Lee, William J Orts, Romana Tabassum, Tawaf Ali Shah, Yousef A Bin Jardan, Turki M Dawoud, Mohammed Bourhia\",\"doi\":\"10.1186/s12896-024-00870-5\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>This study used conservative one variable-at-a-time study and statistical surface response methods to increase the yields of an extracellular thermostable protease secreted by a newly identified thermophilic Bacillus subtilis BSP strain. Using conventional optimization techniques, physical parameters in submerged fermentation were adjusted at the shake flask level to reach 184 U/mL. These physicochemical parameters were further optimized by statistical surface response methodology using Box Behnken design, and the protease yield increased to 295 U/mL. The protease was purified and characterized biochemically. Both Ca<sup>2+</sup> and Fe<sup>2+</sup> increased the activity of the 36 kDa protease enzyme. Based on its strong inhibition by ethylenediaminetetracetate (EDTA), the enzyme was confirmed to be a metalloprotease. The protease was also resistant to various organic solvents (benzene, ethanol, methanol), surfactants (Triton X-100), sodium dodecyl sulfate (SDS), Tween 20, Tween-80 and oxidants hydrogen per oxide (H<sub>2</sub>O<sub>2</sub>). Characteristics, such as tolerance to high SDS and H<sub>2</sub>O<sub>2</sub> concentrations, indicate that this protease has potential applications in the pharmaceutical and detergent industries.</p>\",\"PeriodicalId\":8905,\"journal\":{\"name\":\"BMC Biotechnology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":3.5000,\"publicationDate\":\"2024-07-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11247832/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"BMC Biotechnology\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.1186/s12896-024-00870-5\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOTECHNOLOGY & APPLIED MICROBIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"BMC Biotechnology","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1186/s12896-024-00870-5","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
引用次数: 0

摘要

本研究采用保守的一次一变量研究和统计表面响应方法来提高新发现的嗜热枯草芽孢杆菌 BSP 菌株分泌的胞外恒温蛋白酶的产量。利用传统的优化技术,在摇瓶水平上调整了浸没发酵的物理参数,使其达到 184 U/mL。利用盒式贝肯设计(Box Behnken design)的统计表面响应方法进一步优化了这些理化参数,蛋白酶产量提高到 295 U/mL。对蛋白酶进行了纯化和生化鉴定。Ca2+ 和 Fe2+ 都能提高 36 kDa 蛋白酶的活性。根据乙二胺四乙酸(EDTA)对该酶的强烈抑制作用,证实该酶是一种金属蛋白酶。该蛋白酶还能抵抗各种有机溶剂(苯、乙醇、甲醇)、表面活性剂(Triton X-100)、十二烷基硫酸钠(SDS)、吐温 20、吐温-80 和氧化剂一氧化氢(H2O2)。它对高浓度 SDS 和 H2O2 的耐受性等特性表明,这种蛋白酶有可能应用于制药和洗涤剂行业。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Characterization of a thermostable protease from Bacillus subtilis BSP strain.

This study used conservative one variable-at-a-time study and statistical surface response methods to increase the yields of an extracellular thermostable protease secreted by a newly identified thermophilic Bacillus subtilis BSP strain. Using conventional optimization techniques, physical parameters in submerged fermentation were adjusted at the shake flask level to reach 184 U/mL. These physicochemical parameters were further optimized by statistical surface response methodology using Box Behnken design, and the protease yield increased to 295 U/mL. The protease was purified and characterized biochemically. Both Ca2+ and Fe2+ increased the activity of the 36 kDa protease enzyme. Based on its strong inhibition by ethylenediaminetetracetate (EDTA), the enzyme was confirmed to be a metalloprotease. The protease was also resistant to various organic solvents (benzene, ethanol, methanol), surfactants (Triton X-100), sodium dodecyl sulfate (SDS), Tween 20, Tween-80 and oxidants hydrogen per oxide (H2O2). Characteristics, such as tolerance to high SDS and H2O2 concentrations, indicate that this protease has potential applications in the pharmaceutical and detergent industries.

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
BMC Biotechnology
BMC Biotechnology 工程技术-生物工程与应用微生物
CiteScore
6.60
自引率
0.00%
发文量
34
审稿时长
2 months
期刊介绍: BMC Biotechnology is an open access, peer-reviewed journal that considers articles on the manipulation of biological macromolecules or organisms for use in experimental procedures, cellular and tissue engineering or in the pharmaceutical, agricultural biotechnology and allied industries.
期刊最新文献
Fabrication of apigenin and adenosine-loaded nanoparticles against doxorubicin-induced myocardial infarction by reducing inflammation and oxidative stress. Limonene encapsulated alginate/collagen as antibiofilm drug against Acinetobacter baumannii. Fusarium verticillioides pigment: production, response surface optimization, gamma irradiation and encapsulation studies. Kinetic and thermodynamic analysis of alizarin Red S biosorption by Alhagi maurorum: a sustainable approach for water treatment. Biological activities of Hypericum spectabile extract optimized using artificial neural network combined with genetic algorithm application.
×
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
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 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 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1