Coupling a recombinant oxidase to catalase through specific noncovalent interaction to improve the oxidation of 5-hydroxymethylfurfural to 2,5-furandicarboxylic acid

Han, Yan; Qu, Wenxin; Feng, Wei

doi:10.1016/j.enzmictec.2021.109895

Cited by 4 publications

(2 citation statements)

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“…To improve the soluble expression of MetHMFO in E. coli, it was fused to an elastin-like polypeptide (ELP) at the C-terminus (ELP-MetHMFO). 141 Interestingly, ELP-MetHMFO exhibited improved stability and tolerance toward H 2 O 2 . ELP-MetHMFO was refused to a glutamic acid-rich leucine zipper motif (Z E ) at the N-terminus, which interacts specifically with an arginine-rich leucine zipper motif (Z R ) that was fused to the C-terminus of CAT.…”

Section: Single-enzyme Catalysismentioning

confidence: 99%

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(Chemo)biocatalytic Upgrading of Biobased Furanic Platforms to Chemicals, Fuels, and Materials: A Comprehensive Review

Zong

2022

ACS Catal.

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Biobased furans, such as furfural, 5-hydroxymethylfurfural, and 2,5-furandicarboxylic acid, are recognized as the top-value platform chemicals in the valorization of biomass to chemicals, fuels, and materials. Biocatalysis has emerged as a promising technique in the chemical and pharmaceutical industries because of exquisite selectivity, mild reaction conditions, environmental friendliness, etc. In this comprehensive review, we summarize the recent advances in (chemo)biocatalytic conversion of biobased furans, based on the reaction types including oxidation, reduction, C–C and C–N bonds formation, esterification, and amidation. Particularly, the biocatalysts and their catalytic mechanisms/pathways are critically discussed to allow the rational design and construction of efficient enzymes/multienzyme systems/chemobiocatalytic systems. Besides, various biocatalyst engineering and reaction engineering strategies are highlighted to intensify the processes. Future research directions are proposed to expand the chemical space of furans as well as to improve the commercial acceptance of biocatalytic processes.

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Section: Single-enzyme Catalysismentioning

confidence: 99%

“…To improve the soluble expression of Met HMFO in E. coli, it was fused to an elastin-like polypeptide (ELP) at the C-terminus (ELP- Met HMFO) . Interestingly, ELP- Met HMFO exhibited improved stability and tolerance toward H 2 O 2 .…”

Section: Catalytic Oxidationmentioning

confidence: 99%