Lactococcus cell envelope proteases enable lactococcal growth in minimal growth media supplemented with high molecular weight proteins of plant and animal origin.

IF 2.2 4区 生物学 Q3 MICROBIOLOGY
Lise Friis Christensen, Ida Nynne Laforce, Judith C M Wolkers-Rooijackers, Martin Steen Mortensen, Eddy J Smid, Egon Bech Hansen
{"title":"Lactococcus cell envelope proteases enable lactococcal growth in minimal growth media supplemented with high molecular weight proteins of plant and animal origin.","authors":"Lise Friis Christensen, Ida Nynne Laforce, Judith C M Wolkers-Rooijackers, Martin Steen Mortensen, Eddy J Smid, Egon Bech Hansen","doi":"10.1093/femsle/fnae019","DOIUrl":null,"url":null,"abstract":"<p><p>Lactic acid bacteria (LAB) have evolved into fastidious microorganisms that require amino acids from environmental sources. Some LAB have cell envelope proteases (CEPs) that drive the proteolysis of high molecular weight proteins like casein in milk. CEP activity is typically studied using casein as the predominant substrate, even though CEPs can hydrolyze other protein sources. Plant protein hydrolysis by LAB has rarely been connected to the activity of specific CEPs. This study aims to show the activity of individual CEPs using LAB growth in a minimal growth medium supplemented with high molecular weight casein or potato proteins. Using Lactococcus cremoris MG1363 as isogenic background to express CEPs, we demonstrate that CEP activity is directly related to growth in the protein-supplemented minimal growth media. Proteolysis is analyzed based on the amino acid release, allowing a comparison of CEP activities and analysis of amino acid utilization by L. cremoris MG1363. This approach provides a basis to analyze CEP activity on plant-based protein substrates as casein alternatives and to compare activity of CEP homologs.</p>","PeriodicalId":12214,"journal":{"name":"Fems Microbiology Letters","volume":null,"pages":null},"PeriodicalIF":2.2000,"publicationDate":"2024-01-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Fems Microbiology Letters","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1093/femsle/fnae019","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"MICROBIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Lactic acid bacteria (LAB) have evolved into fastidious microorganisms that require amino acids from environmental sources. Some LAB have cell envelope proteases (CEPs) that drive the proteolysis of high molecular weight proteins like casein in milk. CEP activity is typically studied using casein as the predominant substrate, even though CEPs can hydrolyze other protein sources. Plant protein hydrolysis by LAB has rarely been connected to the activity of specific CEPs. This study aims to show the activity of individual CEPs using LAB growth in a minimal growth medium supplemented with high molecular weight casein or potato proteins. Using Lactococcus cremoris MG1363 as isogenic background to express CEPs, we demonstrate that CEP activity is directly related to growth in the protein-supplemented minimal growth media. Proteolysis is analyzed based on the amino acid release, allowing a comparison of CEP activities and analysis of amino acid utilization by L. cremoris MG1363. This approach provides a basis to analyze CEP activity on plant-based protein substrates as casein alternatives and to compare activity of CEP homologs.

乳球菌细胞包膜蛋白酶能使乳球菌在补充了动植物来源的高分子量蛋白质的最小生长培养基中生长。
乳酸菌(LAB)已进化成需要从环境中获取氨基酸的快速微生物。一些 LAB 具有细胞包膜蛋白酶(CEPs),能驱动高分子量蛋白质(如牛奶中的酪蛋白)的蛋白水解。尽管 CEPs 也能水解其他蛋白质来源,但研究 CEP 活性时通常以酪蛋白为主要底物。酵母菌对植物蛋白的水解很少与特定 CEP 的活性联系起来。本研究旨在利用酵母菌在添加了高分子量酪蛋白或马铃薯蛋白的最小生长培养基中的生长情况,展示单个 CEP 的活性。我们使用 Cremoris MG1363 乳球菌作为表达 CEPs 的同源背景,证明 CEP 活性与蛋白质补充的最小生长培养基中的生长直接相关。根据氨基酸释放量分析蛋白质分解,可以比较 CEP 活性并分析 Cremoris MG1363 对氨基酸的利用。这种方法为分析 CEP 在作为酪蛋白替代物的植物性蛋白质底物上的活性以及比较 CEP 同源物的活性提供了基础。
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
Fems Microbiology Letters
Fems Microbiology Letters 生物-微生物学
CiteScore
4.30
自引率
0.00%
发文量
112
审稿时长
1.9 months
期刊介绍: FEMS Microbiology Letters gives priority to concise papers that merit rapid publication by virtue of their originality, general interest and contribution to new developments in microbiology. All aspects of microbiology, including virology, are covered. 2019 Impact Factor: 1.987, Journal Citation Reports (Source Clarivate, 2020) Ranking: 98/135 (Microbiology) The journal is divided into eight Sections: Physiology and Biochemistry (including genetics, molecular biology and ‘omic’ studies) Food Microbiology (from food production and biotechnology to spoilage and food borne pathogens) Biotechnology and Synthetic Biology Pathogens and Pathogenicity (including medical, veterinary, plant and insect pathogens – particularly those relating to food security – with the exception of viruses) Environmental Microbiology (including ecophysiology, ecogenomics and meta-omic studies) Virology (viruses infecting any organism, including Bacteria and Archaea) Taxonomy and Systematics (for publication of novel taxa, taxonomic reclassifications and reviews of a taxonomic nature) Professional Development (including education, training, CPD, research assessment frameworks, research and publication metrics, best-practice, careers and history of microbiology) If you are unsure which Section is most appropriate for your manuscript, for example in the case of transdisciplinary studies, we recommend that you contact the Editor-In-Chief by email prior to submission. Our scope includes any type of microorganism - all members of the Bacteria and the Archaea and microbial members of the Eukarya (yeasts, filamentous fungi, microbial algae, protozoa, oomycetes, myxomycetes, etc.) as well as all viruses.
×
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