碳水化合物酯酶参与人体肠道菌群对食物成分的去乙酰化。

IF 5.6 2区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY Essays in biochemistry Pub Date : 2023-04-18 DOI:10.1042/EBC20220161
Sabina Leanti La Rosa, Lars J Lindstad, Bjørge Westereng
{"title":"碳水化合物酯酶参与人体肠道菌群对食物成分的去乙酰化。","authors":"Sabina Leanti La Rosa,&nbsp;Lars J Lindstad,&nbsp;Bjørge Westereng","doi":"10.1042/EBC20220161","DOIUrl":null,"url":null,"abstract":"<p><p>Non-carbohydrate modifications such as acetylations are widespread in food stuffs as well as they play important roles in diverse biological processes. These modifications meet the gut environment and are removed from their carbohydrate substrates by the resident microbiota. Among the most abundant modifications are O-acetylations, contributing to polysaccharides physico-chemical properties such as viscosity and gelling ability, as well as reducing accessibility for glycosyl hydrolases, and thus hindering polysaccharide degradation. Of particular note, O-acetylations increase the overall complexity of a polymer, thus requiring a more advanced degrading machinery for microbes to utilize it. This minireview describes acetylesterases from the gut microbiota that deacetylate various food polysaccharides, either as natural components of food, ingredients, stabilizers of microbial origin, or as part of microbes for food and beverage preparations. These enzymes include members belonging to at least 8 families in the CAZy database, as well as a large number of biochemically characterized esterases that have not been classified yet. Despite different structural folds, most of these acetylesterases have a common acid-base mechanism and belong to the SGNH hydrolase superfamily. We highlight examples of acetylesterases that are highly specific to one substrate and to the position of the acetyl group on the glycosyl residue of the carbohydrate, while other members that have more broad substrate specificity. Current research aimed at unveiling the functions and regioselectivity of acetylesterases will help providing fundamental mechanistic understanding on how dietary components are utilized in the human gut and will aid developing applications of these enzymes to manufacture novel industrial products.</p>","PeriodicalId":11812,"journal":{"name":"Essays in biochemistry","volume":"67 3","pages":"443-454"},"PeriodicalIF":5.6000,"publicationDate":"2023-04-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/1d/18/ebc-67-ebc20220161.PMC10154613.pdf","citationCount":"2","resultStr":"{\"title\":\"Carbohydrate esterases involved in deacetylation of food components by the human gut microbiota.\",\"authors\":\"Sabina Leanti La Rosa,&nbsp;Lars J Lindstad,&nbsp;Bjørge Westereng\",\"doi\":\"10.1042/EBC20220161\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Non-carbohydrate modifications such as acetylations are widespread in food stuffs as well as they play important roles in diverse biological processes. These modifications meet the gut environment and are removed from their carbohydrate substrates by the resident microbiota. Among the most abundant modifications are O-acetylations, contributing to polysaccharides physico-chemical properties such as viscosity and gelling ability, as well as reducing accessibility for glycosyl hydrolases, and thus hindering polysaccharide degradation. Of particular note, O-acetylations increase the overall complexity of a polymer, thus requiring a more advanced degrading machinery for microbes to utilize it. This minireview describes acetylesterases from the gut microbiota that deacetylate various food polysaccharides, either as natural components of food, ingredients, stabilizers of microbial origin, or as part of microbes for food and beverage preparations. These enzymes include members belonging to at least 8 families in the CAZy database, as well as a large number of biochemically characterized esterases that have not been classified yet. Despite different structural folds, most of these acetylesterases have a common acid-base mechanism and belong to the SGNH hydrolase superfamily. We highlight examples of acetylesterases that are highly specific to one substrate and to the position of the acetyl group on the glycosyl residue of the carbohydrate, while other members that have more broad substrate specificity. Current research aimed at unveiling the functions and regioselectivity of acetylesterases will help providing fundamental mechanistic understanding on how dietary components are utilized in the human gut and will aid developing applications of these enzymes to manufacture novel industrial products.</p>\",\"PeriodicalId\":11812,\"journal\":{\"name\":\"Essays in biochemistry\",\"volume\":\"67 3\",\"pages\":\"443-454\"},\"PeriodicalIF\":5.6000,\"publicationDate\":\"2023-04-18\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/1d/18/ebc-67-ebc20220161.PMC10154613.pdf\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Essays in biochemistry\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1042/EBC20220161\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Essays in biochemistry","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1042/EBC20220161","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 2

摘要

非碳水化合物修饰如乙酰化在食品中广泛存在,并且在各种生物过程中起着重要作用。这些修饰符合肠道环境,并被常驻微生物群从碳水化合物底物中去除。其中最丰富的修饰是o-乙酰化,它有助于多糖的物理化学性质,如粘度和胶凝能力,以及降低糖基水解酶的可及性,从而阻碍多糖的降解。特别值得注意的是,o -乙酰化增加了聚合物的整体复杂性,因此需要更先进的降解机制供微生物利用。这篇综述介绍了来自肠道微生物群的乙酰酯酶,它可以将各种食物多糖脱乙酰,作为食物的天然成分、成分、微生物来源的稳定剂,或作为食品和饮料制剂中微生物的一部分。这些酶包括CAZy数据库中至少8个家族的成员,以及大量尚未分类的具有生化特征的酯酶。尽管结构褶皱不同,但这些乙酰酯酶大多具有共同的酸碱机制,属于SGNH水解酶超家族。我们重点介绍了乙酰酯酶的例子,这些酶对一种底物和碳水化合物糖基残基上乙酰基的位置具有高度特异性,而其他成员则具有更广泛的底物特异性。目前的研究旨在揭示乙酰酯酶的功能和区域选择性,这将有助于提供关于膳食成分如何在人体肠道中被利用的基本机制理解,并将有助于开发这些酶在制造新型工业产品中的应用。
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
Carbohydrate esterases involved in deacetylation of food components by the human gut microbiota.

Non-carbohydrate modifications such as acetylations are widespread in food stuffs as well as they play important roles in diverse biological processes. These modifications meet the gut environment and are removed from their carbohydrate substrates by the resident microbiota. Among the most abundant modifications are O-acetylations, contributing to polysaccharides physico-chemical properties such as viscosity and gelling ability, as well as reducing accessibility for glycosyl hydrolases, and thus hindering polysaccharide degradation. Of particular note, O-acetylations increase the overall complexity of a polymer, thus requiring a more advanced degrading machinery for microbes to utilize it. This minireview describes acetylesterases from the gut microbiota that deacetylate various food polysaccharides, either as natural components of food, ingredients, stabilizers of microbial origin, or as part of microbes for food and beverage preparations. These enzymes include members belonging to at least 8 families in the CAZy database, as well as a large number of biochemically characterized esterases that have not been classified yet. Despite different structural folds, most of these acetylesterases have a common acid-base mechanism and belong to the SGNH hydrolase superfamily. We highlight examples of acetylesterases that are highly specific to one substrate and to the position of the acetyl group on the glycosyl residue of the carbohydrate, while other members that have more broad substrate specificity. Current research aimed at unveiling the functions and regioselectivity of acetylesterases will help providing fundamental mechanistic understanding on how dietary components are utilized in the human gut and will aid developing applications of these enzymes to manufacture novel industrial products.

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
Essays in biochemistry
Essays in biochemistry 生物-生化与分子生物学
CiteScore
10.50
自引率
0.00%
发文量
105
审稿时长
>12 weeks
期刊介绍: Essays in Biochemistry publishes short, digestible reviews from experts highlighting recent key topics in biochemistry and the molecular biosciences. Written to be accessible for those not yet immersed in the subject, each article is an up-to-date, self-contained summary of the topic. Bridging the gap between the latest research and established textbooks, Essays in Biochemistry will tell you what you need to know to begin exploring the field, as each article includes the top take-home messages as summary points. Each issue of the journal is guest edited by a key opinion leader in the area, and whether you are continuing your studies or moving into a new research area, the Journal gives a complete picture in one place. Essays in Biochemistry is proud to publish Understanding Biochemistry, an essential online resource for post-16 students, teachers and undergraduates. Providing up-to-date overviews of key concepts in biochemistry and the molecular biosciences, the Understanding Biochemistry issues of Essays in Biochemistry are published annually in October.
期刊最新文献
NUAK: never underestimate a kinase. New developments in AMPK and mTORC1 cross-talk. How mass spectrometry can be exploited to study AMPK. New concepts in the roles of AMPK in adipocyte stem cell biology. Does AMPK bind glycogen in skeletal muscle or is the relationship correlative?
×
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