Synergy between processive cellulases in Ruminoccocus albus

IF 3.4 3区生物学 Q2 BIOTECHNOLOGY & APPLIED MICROBIOLOGY Enzyme and Microbial Technology Pub Date : 2025-02-18 DOI:10.1016/j.enzmictec.2025.110610

Alem Storani , Alberto A. Iglesias, Sergio A. Guerrero

{"title":"Synergy between processive cellulases in Ruminoccocus albus","authors":"Alem Storani , Alberto A. Iglesias, Sergio A. Guerrero","doi":"10.1016/j.enzmictec.2025.110610","DOIUrl":null,"url":null,"abstract":"<div><div>Endoglucanases (EGs), cellobiohydrolases (CBHs), and β-glucosidases are essential components in enzymatic degradation of cellulose. We analyzed the glycosyl hydrolases from families GH5 and GH48 from <em>Ruminococcus albus</em> 8 (<em>Ral</em>Cel5G and <em>Ral</em>Cel48A). Both enzymes feature a catalytic motif and a carbohydrate binding domain from family 37 (CBM37). <em>Ral</em>Cel5G also exhibited a second CBM37 with lower similarity. As a result, <em>Ral</em>Cel5G showed higher binding affinity toward insoluble substrates and broader recognition capacity. Kinetic characterization using different cellulosic substrates and reaction product analysis confirmed <em>Ral</em>Cel5G as a processive EG while <em>Ral</em>Cel48A is a CBH. Interestingly, we found a synergistic effect on their activity at a low EG to CBH ratio, despite the processive activity of <em>Ral</em>Cel5G. Furthermore, the lignocellulose degradation capacity was improved by supplementing the cellulases with hemicellulase <em>Ral</em>Xyn10A. These results provide valuable information about the interaction between processive EG and conventional CBH, necessary for the rational design of enzyme cocktails for optimized biomass processing.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"186 ","pages":"Article 110610"},"PeriodicalIF":3.4000,"publicationDate":"2025-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Enzyme and Microbial Technology","FirstCategoryId":"5","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0141022925000304","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}

引用次数: 0

Abstract

Endoglucanases (EGs), cellobiohydrolases (CBHs), and β-glucosidases are essential components in enzymatic degradation of cellulose. We analyzed the glycosyl hydrolases from families GH5 and GH48 from Ruminococcus albus 8 (RalCel5G and RalCel48A). Both enzymes feature a catalytic motif and a carbohydrate binding domain from family 37 (CBM37). RalCel5G also exhibited a second CBM37 with lower similarity. As a result, RalCel5G showed higher binding affinity toward insoluble substrates and broader recognition capacity. Kinetic characterization using different cellulosic substrates and reaction product analysis confirmed RalCel5G as a processive EG while RalCel48A is a CBH. Interestingly, we found a synergistic effect on their activity at a low EG to CBH ratio, despite the processive activity of RalCel5G. Furthermore, the lignocellulose degradation capacity was improved by supplementing the cellulases with hemicellulase RalXyn10A. These results provide valuable information about the interaction between processive EG and conventional CBH, necessary for the rational design of enzyme cocktails for optimized biomass processing.

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

求助全文

约1分钟内获得全文去求助

来源期刊

Enzyme and Microbial Technology 生物-生物工程与应用微生物

CiteScore

7.60

自引率

5.90%

发文量

142

审稿时长

38 days

期刊介绍： Enzyme and Microbial Technology is an international, peer-reviewed journal publishing original research and reviews, of biotechnological significance and novelty, on basic and applied aspects of the science and technology of processes involving the use of enzymes, micro-organisms, animal cells and plant cells. We especially encourage submissions on: Biocatalysis and the use of Directed Evolution in Synthetic Biology and Biotechnology Biotechnological Production of New Bioactive Molecules, Biomaterials, Biopharmaceuticals, and Biofuels New Imaging Techniques and Biosensors, especially as applicable to Healthcare and Systems Biology New Biotechnological Approaches in Genomics, Proteomics and Metabolomics Metabolic Engineering, Biomolecular Engineering and Nanobiotechnology Manuscripts which report isolation, purification, immobilization or utilization of organisms or enzymes which are already well-described in the literature are not suitable for publication in EMT, unless their primary purpose is to report significant new findings or approaches which are of broad biotechnological importance. Similarly, manuscripts which report optimization studies on well-established processes are inappropriate. EMT does not accept papers dealing with mathematical modeling unless they report significant, new experimental data.