{"title":"Simultaneous production of linear α-olefins and 2,5-furandicarboxylic acid by combining two recombinant enzymes OleT-ELP and HMFO-ELP","authors":"Yaqi Fu , Siyu Mao , Tianyue Liao , Wei Feng","doi":"10.1016/j.enzmictec.2025.110637","DOIUrl":null,"url":null,"abstract":"<div><div>The enzyme OleT can utilize H<sub>2</sub>O<sub>2</sub> as the co-substrate, and this biocatalysis is an H<sub>2</sub>O<sub>2</sub>-driven enzymatic catalysis. In this work, OleT was recombinated by being fused to an elastin-like polypeptide (ELP). The recombinant enzyme OleT-ELP exhibits higher stability and resistance to H<sub>2</sub>O<sub>2</sub> interference compared to native OleT. OleT-ELP showed improved catalytic efficiency in producing α-olefins via fatty acid decarboxylation. The recombinant 5-hydroxymethylfurfural oxidase <strong>(</strong>HMFO-ELP) catalyzes the oxidation of 5-hydroxymethylfurfural (HMF) to 2,5-furandicarboxylic acid (FDCA), generating H<sub>2</sub>O<sub>2</sub> as a byproduct. Combining OleT-ELP with HMFO-ELP enabled simultaneous conversion of fatty acids and HMF. The <em>in situ</em> H<sub>2</sub>O<sub>2</sub> generated by HMFO-ELP was transferred to OleT-ELP, enhancing catalytic efficiencies for both α-olefins and FDCA production.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"188 ","pages":"Article 110637"},"PeriodicalIF":3.4000,"publicationDate":"2025-03-22","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/S0141022925000572","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
The enzyme OleT can utilize H2O2 as the co-substrate, and this biocatalysis is an H2O2-driven enzymatic catalysis. In this work, OleT was recombinated by being fused to an elastin-like polypeptide (ELP). The recombinant enzyme OleT-ELP exhibits higher stability and resistance to H2O2 interference compared to native OleT. OleT-ELP showed improved catalytic efficiency in producing α-olefins via fatty acid decarboxylation. The recombinant 5-hydroxymethylfurfural oxidase (HMFO-ELP) catalyzes the oxidation of 5-hydroxymethylfurfural (HMF) to 2,5-furandicarboxylic acid (FDCA), generating H2O2 as a byproduct. Combining OleT-ELP with HMFO-ELP enabled simultaneous conversion of fatty acids and HMF. The in situ H2O2 generated by HMFO-ELP was transferred to OleT-ELP, enhancing catalytic efficiencies for both α-olefins and FDCA production.
期刊介绍:
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