Recent trends in production and potential applications of microbial amylases: A comprehensive review

IF 1.4 4区 生物学 Q4 BIOCHEMICAL RESEARCH METHODS
Zain Ali , Muhammad Abdullah , Muhammad Talha Yasin , Kinza Amanat , Mohsin Sultan , Aqdas Rahim , Fatima Sarwar
{"title":"Recent trends in production and potential applications of microbial amylases: A comprehensive review","authors":"Zain Ali ,&nbsp;Muhammad Abdullah ,&nbsp;Muhammad Talha Yasin ,&nbsp;Kinza Amanat ,&nbsp;Mohsin Sultan ,&nbsp;Aqdas Rahim ,&nbsp;Fatima Sarwar","doi":"10.1016/j.pep.2024.106640","DOIUrl":null,"url":null,"abstract":"<div><div>α-amylases are vital biocatalysts that constitute a billion-dollar industry with a substantial and enduring global demand. Amylases hydrolyze the α-1,4-glycosidic linkages in starch polymers to generate maltose and malto-oligosaccharides subunits. Amylases are key enzymes that have promising applications in various industrial processes ranging from pharmaceutical, pulp and paper, textile food industries to bioremediation and biofuel sectors. Microbial enzymes have been widely used in industrial applications owing to their ease of availability, cost-effectiveness and better stability at extreme temperatures and pH. α-amylases derived from distinct microbial origins exhibit diverse characteristics, which make them suitable for specific applications. The routine application of immobilized enzymes has become a standard practice in the production of numerous industrial products across the pharmaceutical, chemical, and food industries. This review details the structural makeup of microbial α-amylase to understand its thermodynamic characteristics, aiming to identify key areas that could be targeted for improving the thermostability, pH tolerance and catalytic activity of α-amylase through various immobilization techniques or specific enzyme engineering methods. Additionally, the review briefly explores the enzyme production strategies, potential sources of α-amylases, and use of cost-effective and sustainable raw materials for enzyme production to obtain α-amylases with unconventional applications in various industrial sectors. Major hurdles, challenges and future prospects involving microbial α-amylases has been briefly discussed by considering its diverse applications in industrial bioprocessing.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"227 ","pages":"Article 106640"},"PeriodicalIF":1.4000,"publicationDate":"2024-12-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Protein expression and purification","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1046592824002122","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}
引用次数: 0

Abstract

α-amylases are vital biocatalysts that constitute a billion-dollar industry with a substantial and enduring global demand. Amylases hydrolyze the α-1,4-glycosidic linkages in starch polymers to generate maltose and malto-oligosaccharides subunits. Amylases are key enzymes that have promising applications in various industrial processes ranging from pharmaceutical, pulp and paper, textile food industries to bioremediation and biofuel sectors. Microbial enzymes have been widely used in industrial applications owing to their ease of availability, cost-effectiveness and better stability at extreme temperatures and pH. α-amylases derived from distinct microbial origins exhibit diverse characteristics, which make them suitable for specific applications. The routine application of immobilized enzymes has become a standard practice in the production of numerous industrial products across the pharmaceutical, chemical, and food industries. This review details the structural makeup of microbial α-amylase to understand its thermodynamic characteristics, aiming to identify key areas that could be targeted for improving the thermostability, pH tolerance and catalytic activity of α-amylase through various immobilization techniques or specific enzyme engineering methods. Additionally, the review briefly explores the enzyme production strategies, potential sources of α-amylases, and use of cost-effective and sustainable raw materials for enzyme production to obtain α-amylases with unconventional applications in various industrial sectors. Major hurdles, challenges and future prospects involving microbial α-amylases has been briefly discussed by considering its diverse applications in industrial bioprocessing.
微生物淀粉酶的生产和潜在应用的最新趋势:综述。
α-淀粉酶是一种重要的生物催化剂,它构成了一个价值数十亿美元的产业,有着巨大而持久的全球需求。淀粉酶水解淀粉聚合物中的α-1,4-糖苷键,生成麦芽糖和麦芽糖低聚糖亚基。淀粉酶是在各种工业过程中具有广阔应用前景的关键酶,从制药、纸浆和造纸、纺织食品工业到生物修复和生物燃料部门。微生物酶由于其易于获得、成本效益和在极端温度和ph下更好的稳定性而广泛应用于工业应用。来源于不同微生物来源的α-淀粉酶表现出不同的特性,这使它们适合于特定的应用。固定化酶的常规应用已成为制药、化工和食品工业中众多工业产品生产的标准做法。本文详细介绍了微生物α-淀粉酶的结构组成,了解其热力学特性,旨在通过各种固定化技术或特定的酶工程方法找到提高α-淀粉酶热稳定性、pH耐受性和催化活性的关键领域。此外,本文还简要探讨了α-淀粉酶的生产策略、α-淀粉酶的潜在来源,以及利用具有成本效益和可持续性的原料生产酶,以获得在各个工业领域具有非常规应用的α-淀粉酶。结合α-淀粉酶在工业生物加工中的多种应用,简要讨论了α-淀粉酶的主要障碍、挑战和未来前景。
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
Protein expression and purification
Protein expression and purification 生物-生化研究方法
CiteScore
3.70
自引率
6.20%
发文量
120
审稿时长
32 days
期刊介绍: Protein Expression and Purification is an international journal providing a forum for the dissemination of new information on protein expression, extraction, purification, characterization, and/or applications using conventional biochemical and/or modern molecular biological approaches and methods, which are of broad interest to the field. The journal does not typically publish repetitive examples of protein expression and purification involving standard, well-established, methods. However, exceptions might include studies on important and/or difficult to express and/or purify proteins and/or studies that include extensive protein characterization, which provide new, previously unpublished information.
×
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