Li Yang , Jia Chen , Kangshun Xie , Kaiwen He , Wenyang Sheng , Mi Zhou , Guangyang Jiang , Yongqiang Tian
{"title":"Effects of deep eutectic solvent on laccase activity and thermal stability","authors":"Li Yang , Jia Chen , Kangshun Xie , Kaiwen He , Wenyang Sheng , Mi Zhou , Guangyang Jiang , Yongqiang Tian","doi":"10.1016/j.biortech.2025.132992","DOIUrl":null,"url":null,"abstract":"<div><div>Eighteen deep eutectic solvent (DES) systems were systematically evaluated to optimize laccase biocatalysis. Five hydrogen bond acceptors (HBAs) significantly enhanced both enzyme activity and thermal stability. The choline dihydrogen phosphate (ChDHP)-glycerol DES yielded the highest activity increase (198 %). Moreover, a 50 % betaine-sorbitol (BS) solution retained 92 % activity after 1 h at 70 °C—55-fold higher than buffer—addressing a key thermal stability challenge. Fluorescence spectroscopy (FS) and molecular docking revealed that DES solutions stabilized laccase’s native structure by forming hydrogen bonds with catalytic center histidine (His) and phenylalanine (Phe) residues. BS-laccase pretreatment increased glucose conversion by 30 % in distillers’ grains (DG) and 54 % in poplar wood (PW). These findings establish DES as a sustainable, low-cost co-solvent that boosts enzymatic efficiency, offering molecular insights into HBA-enzyme interactions to guide biocatalytic system design for circular bioeconomy.</div></div>","PeriodicalId":258,"journal":{"name":"Bioresource Technology","volume":"436 ","pages":"Article 132992"},"PeriodicalIF":9.7000,"publicationDate":"2025-07-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioresource Technology","FirstCategoryId":"5","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0960852425009587","RegionNum":1,"RegionCategory":"环境科学与生态学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURAL ENGINEERING","Score":null,"Total":0}
引用次数: 0
Abstract
Eighteen deep eutectic solvent (DES) systems were systematically evaluated to optimize laccase biocatalysis. Five hydrogen bond acceptors (HBAs) significantly enhanced both enzyme activity and thermal stability. The choline dihydrogen phosphate (ChDHP)-glycerol DES yielded the highest activity increase (198 %). Moreover, a 50 % betaine-sorbitol (BS) solution retained 92 % activity after 1 h at 70 °C—55-fold higher than buffer—addressing a key thermal stability challenge. Fluorescence spectroscopy (FS) and molecular docking revealed that DES solutions stabilized laccase’s native structure by forming hydrogen bonds with catalytic center histidine (His) and phenylalanine (Phe) residues. BS-laccase pretreatment increased glucose conversion by 30 % in distillers’ grains (DG) and 54 % in poplar wood (PW). These findings establish DES as a sustainable, low-cost co-solvent that boosts enzymatic efficiency, offering molecular insights into HBA-enzyme interactions to guide biocatalytic system design for circular bioeconomy.
期刊介绍:
Bioresource Technology publishes original articles, review articles, case studies, and short communications covering the fundamentals, applications, and management of bioresource technology. The journal seeks to advance and disseminate knowledge across various areas related to biomass, biological waste treatment, bioenergy, biotransformations, bioresource systems analysis, and associated conversion or production technologies.
Topics include:
• Biofuels: liquid and gaseous biofuels production, modeling and economics
• Bioprocesses and bioproducts: biocatalysis and fermentations
• Biomass and feedstocks utilization: bioconversion of agro-industrial residues
• Environmental protection: biological waste treatment
• Thermochemical conversion of biomass: combustion, pyrolysis, gasification, catalysis.