Synergism of Endo and Exo-α-1,3-Glucanases in α-1,3-Glucan Degradation: A Kinetic Study

IF 7.1 1区 化学 Q1 CHEMISTRY, MULTIDISCIPLINARY ACS Sustainable Chemistry & Engineering Pub Date : 2024-05-25 DOI:10.1021/acssuschemeng.4c01469
Zhe Dong, Peng Zhang, Slavko Kralj, Yu Ji* and Ulrich Schwaneberg*, 
{"title":"Synergism of Endo and Exo-α-1,3-Glucanases in α-1,3-Glucan Degradation: A Kinetic Study","authors":"Zhe Dong,&nbsp;Peng Zhang,&nbsp;Slavko Kralj,&nbsp;Yu Ji* and Ulrich Schwaneberg*,&nbsp;","doi":"10.1021/acssuschemeng.4c01469","DOIUrl":null,"url":null,"abstract":"<p >Biobased materials are promising alternatives to traditional fossil-derived synthetic polymers to mitigate greenhouse gas emissions and to provide end-of-life benefits addressing increasing environmental concerns. Biobased polymers with advantaged degradation and reuse characteristics have attracted increasing attention. In this work, a dual-enzyme system (combining endo α-1,3-glucanase Agl-ST from <i>Streptomyces thermodiastaticus</i> HF 3–3 and exo α-1,3-glucanase YgjK from <i>Escherichia coli</i> K12) was identified for the targeted degradation of α-1,3-glucan. The effects of pH, metal ions, enzyme concentration, temperature, and reaction time were investigated to assess the degradation characteristics of α-1,3-glucan using the synergistic enzyme system. After degradation under model conditions for 10 h, the dual-enzyme system achieved a weight loss rate of 29%, releasing 4.0 mM reducing sugar from 1% α-1,3-glucan. Binding behavior and degradation kinetics of α-1,3-glucanase on α-1,3-glucan were studied by a quartz crystal microbalance with dissipation monitoring. This dual-α-1,3-glucanase enzyme cocktail is a promising example for efficient biobased α-1,3-glucan polymer degradation, thereby contributing toward the concept of a circular economy.</p>","PeriodicalId":25,"journal":{"name":"ACS Sustainable Chemistry & Engineering","volume":"12 24","pages":"9123–9132"},"PeriodicalIF":7.1000,"publicationDate":"2024-05-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"ACS Sustainable Chemistry & Engineering","FirstCategoryId":"92","ListUrlMain":"https://pubs.acs.org/doi/10.1021/acssuschemeng.4c01469","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 0

Abstract

Biobased materials are promising alternatives to traditional fossil-derived synthetic polymers to mitigate greenhouse gas emissions and to provide end-of-life benefits addressing increasing environmental concerns. Biobased polymers with advantaged degradation and reuse characteristics have attracted increasing attention. In this work, a dual-enzyme system (combining endo α-1,3-glucanase Agl-ST from Streptomyces thermodiastaticus HF 3–3 and exo α-1,3-glucanase YgjK from Escherichia coli K12) was identified for the targeted degradation of α-1,3-glucan. The effects of pH, metal ions, enzyme concentration, temperature, and reaction time were investigated to assess the degradation characteristics of α-1,3-glucan using the synergistic enzyme system. After degradation under model conditions for 10 h, the dual-enzyme system achieved a weight loss rate of 29%, releasing 4.0 mM reducing sugar from 1% α-1,3-glucan. Binding behavior and degradation kinetics of α-1,3-glucanase on α-1,3-glucan were studied by a quartz crystal microbalance with dissipation monitoring. This dual-α-1,3-glucanase enzyme cocktail is a promising example for efficient biobased α-1,3-glucan polymer degradation, thereby contributing toward the concept of a circular economy.

Abstract Image

Abstract Image

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
内切酶和外切酶在α-1,3-葡聚糖降解过程中的协同作用:动力学研究
生物基材料是传统化石源合成聚合物的理想替代品,可减少温室气体排放,并在报废时为解决日益严重的环境问题带来益处。具有良好降解和再利用特性的生物基聚合物越来越受到关注。在这项工作中,研究人员发现了一种双酶系统(将热淀粉链霉菌 HF 3-3 中的内α-1,3-葡聚糖酶 Agl-ST 和大肠杆菌 K12 中的外α-1,3-葡聚糖酶 YgjK 结合在一起),可定向降解α-1,3-葡聚糖。研究了 pH 值、金属离子、酶浓度、温度和反应时间对协同酶系统降解α-1,3-葡聚糖特性的影响。在模型条件下降解 10 小时后,双酶体系的失重率达到 29%,从 1% α-1,3-葡聚糖中释放出 4.0 mM 还原糖。通过石英晶体微天平和耗散监测研究了α-1,3-葡聚糖酶对α-1,3-葡聚糖的结合行为和降解动力学。这种双α-1,3-葡聚糖酶鸡尾酒是高效降解生物基α-1,3-葡聚糖聚合物的一个很有前景的例子,从而有助于实现循环经济的概念。
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 去求助
来源期刊
ACS Sustainable Chemistry & Engineering
ACS Sustainable Chemistry & Engineering CHEMISTRY, MULTIDISCIPLINARY-ENGINEERING, CHEMICAL
CiteScore
13.80
自引率
4.80%
发文量
1470
审稿时长
1.7 months
期刊介绍: ACS Sustainable Chemistry & Engineering is a prestigious weekly peer-reviewed scientific journal published by the American Chemical Society. Dedicated to advancing the principles of green chemistry and green engineering, it covers a wide array of research topics including green chemistry, green engineering, biomass, alternative energy, and life cycle assessment. The journal welcomes submissions in various formats, including Letters, Articles, Features, and Perspectives (Reviews), that address the challenges of sustainability in the chemical enterprise and contribute to the advancement of sustainable practices. Join us in shaping the future of sustainable chemistry and engineering.
期刊最新文献
In Situ Phase Transformation-Induced High-Activity Nickel–Molybdenum Catalyst for Enhancing High-Current-Density Water/Seawater Splitting Investigation on the Impact of Coexisting Component for the Catalytic Hydrogenolysis of Cellulose in Bagasse to 2,5-Hexanedione Enhanced Oxygen Reduction Reaction Kinetics of Li-Containing Oxide as a High-Performance Cathode for Solid Oxide Fuel Cells Through Synergistic Li Volatilization and Anion Doping Exploring the Enhancement on CO2 Mineralization of Solid Wastes via Amine-Looping Preparation of Hydrogen Storage Liquid Fuel by Biomass-Based Syngas from Corn Straw over a C60 Modified Hydrophobic Catalyst
×
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