Novel domain-structure-containing chitinases A and B of Bacillus velezensis produced by recombinant Escherichia coli cells: Synergism on chitin degradation and their potential in suppressing Candida albicans cell germination

IF 3.5 Q3 Biochemistry, Genetics and Molecular Biology
{"title":"Novel domain-structure-containing chitinases A and B of Bacillus velezensis produced by recombinant Escherichia coli cells: Synergism on chitin degradation and their potential in suppressing Candida albicans cell germination","authors":"","doi":"10.1016/j.jgeb.2024.100402","DOIUrl":null,"url":null,"abstract":"<div><p><em>Bacillus velezensis</em> RB.IBE29 harbors two chitinases belonging to the glycoside hydrolase family 18 and exhibiting a novel domain structure. The roles of these chitinases in crop production have been reported; nevertheless, their contribution to controlling human pathogens is unknown. In this initial work, the chitinases A (BvChiA) and B (BvChiB) of strain RB.IBE29 were produced in recombinant <em>Escherichia coli</em> BL21-CodonPlus (DE3)-RIPL cells and subsequently purified using HisTrap FF column. The purified BvChiA and BvChiB exhibited the highest chitinase and binding activities against colloidal chitin. Combining both chitinases for the hydrolysis of powdered chitin increased the reducing sugar content by 88.7 %. Moreover, the purified chitinases remarkably suppressed the germination of <em>Candida albicans</em> VTCC 20568 (=JCM 2070) cells. These results indicated that the novel domain-structure-containing chitinases of strain RB.IBE29 have great potential and can be further developed as a novel therapeutic agent against human pathogenic <em>C. albicans</em>.</p></div>","PeriodicalId":53463,"journal":{"name":"Journal of Genetic Engineering and Biotechnology","volume":null,"pages":null},"PeriodicalIF":3.5000,"publicationDate":"2024-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1687157X24001057/pdfft?md5=61ce122ba96e17d2dba767dce5a11731&pid=1-s2.0-S1687157X24001057-main.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Genetic Engineering and Biotechnology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1687157X24001057","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
引用次数: 0

Abstract

Bacillus velezensis RB.IBE29 harbors two chitinases belonging to the glycoside hydrolase family 18 and exhibiting a novel domain structure. The roles of these chitinases in crop production have been reported; nevertheless, their contribution to controlling human pathogens is unknown. In this initial work, the chitinases A (BvChiA) and B (BvChiB) of strain RB.IBE29 were produced in recombinant Escherichia coli BL21-CodonPlus (DE3)-RIPL cells and subsequently purified using HisTrap FF column. The purified BvChiA and BvChiB exhibited the highest chitinase and binding activities against colloidal chitin. Combining both chitinases for the hydrolysis of powdered chitin increased the reducing sugar content by 88.7 %. Moreover, the purified chitinases remarkably suppressed the germination of Candida albicans VTCC 20568 (=JCM 2070) cells. These results indicated that the novel domain-structure-containing chitinases of strain RB.IBE29 have great potential and can be further developed as a novel therapeutic agent against human pathogenic C. albicans.

重组大肠杆菌细胞产生的新型含结构域的 Velezensis 杆菌几丁质酶 A 和 B:几丁质降解的协同作用及其抑制白色念珠菌细胞萌发的潜力
RB.IBE29含有两种属于糖苷水解酶家族18的几丁质酶,并表现出一种新颖的结构域。这些几丁质酶在作物生产中的作用已有报道,但它们在控制人类病原体方面的作用尚不清楚。在这项初步工作中,在重组 BL21-CodonPlus (DE3)-RIPL 细胞中产生了菌株 RB.IBE29 的几丁质酶 A(BvChiA)和 B(BvChiB),随后使用 HisTrap FF 柱进行纯化。纯化的 BvChiA 和 BvChiB 对胶体几丁质具有最高的几丁质酶活性和结合活性。结合使用这两种几丁质酶水解粉末状几丁质可使还原糖含量提高 88.7%。此外,纯化的几丁质酶明显抑制了 VTCC 20568(=JCM 2070)细胞的萌发。这些结果表明,RB.IBE29菌株的新型含结构域的几丁质酶具有很大的潜力,可进一步开发为针对人类病原菌的新型治疗剂。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Journal of Genetic Engineering and Biotechnology
Journal of Genetic Engineering and Biotechnology Biochemistry, Genetics and Molecular Biology-Biotechnology
CiteScore
5.70
自引率
5.70%
发文量
159
审稿时长
16 weeks
期刊介绍: Journal of genetic engineering and biotechnology is devoted to rapid publication of full-length research papers that leads to significant contribution in advancing knowledge in genetic engineering and biotechnology and provide novel perspectives in this research area. JGEB includes all major themes related to genetic engineering and recombinant DNA. The area of interest of JGEB includes but not restricted to: •Plant genetics •Animal genetics •Bacterial enzymes •Agricultural Biotechnology, •Biochemistry, •Biophysics, •Bioinformatics, •Environmental Biotechnology, •Industrial Biotechnology, •Microbial biotechnology, •Medical Biotechnology, •Bioenergy, Biosafety, •Biosecurity, •Bioethics, •GMOS, •Genomic, •Proteomic JGEB accepts
×
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