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Oxidation of 5-hydroxymethylfurfural with a novel aryl alcohol oxidase from Mycobacterium sp. MS1601

Sayed, Mahmoud LU orcid ; Gaber, Yasser LU ; Junghus, Fredrik LU ; Martín, Eric Valdés ; Pyo, Sang-Hyun LU and Hatti-Kaul, Rajni LU (2022) In Microbial Biotechnology 15(8). p.2176-2190
Abstract

Bio-based 5-hydroxymethylfurfural (HMF) serves as an important platform for several chemicals, among which 2,5-furan dicarboxylic acid (FDCA) has attracted considerable interest as a monomer for the production of polyethylene furanoate (PEF), a potential alternative for fossil-based polyethylene terephthalate (PET). This study is based on the HMF oxidizing activity shown by Mycobacterium sp. MS 1601 cells and investigation of the enzyme catalysing the oxidation. The Mycobacterium whole cells oxidized the HMF to FDCA (60% yield) and hydroxymethyl furan carboxylic acid (HMFCA). A gene encoding a novel bacterial aryl alcohol oxidase, hereinafter MycspAAO, was identified in the genome and was cloned and expressed in... (More)

Bio-based 5-hydroxymethylfurfural (HMF) serves as an important platform for several chemicals, among which 2,5-furan dicarboxylic acid (FDCA) has attracted considerable interest as a monomer for the production of polyethylene furanoate (PEF), a potential alternative for fossil-based polyethylene terephthalate (PET). This study is based on the HMF oxidizing activity shown by Mycobacterium sp. MS 1601 cells and investigation of the enzyme catalysing the oxidation. The Mycobacterium whole cells oxidized the HMF to FDCA (60% yield) and hydroxymethyl furan carboxylic acid (HMFCA). A gene encoding a novel bacterial aryl alcohol oxidase, hereinafter MycspAAO, was identified in the genome and was cloned and expressed in Escherichia coli Bl21 (DE3). The purified MycspAAO displayed activity against several alcohols and aldehydes; 3,5 dimethoxy benzyl alcohol (veratryl alcohol) was the best substrate among those tested followed by HMF. 5-Hydroxymethylfurfural was converted to 5-formyl-2-furoic acid (FFCA) via diformyl furan (DFF) with optimal activity at pH 8 and 30–40°C. FDCA formation was observed during long reaction time with low HMF concentration. Mutagenesis of several amino acids shaping the active site and evaluation of the variants showed Y444F to have around 3-fold higher kcat/Km and ~1.7-fold lower Km with HMF.

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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Microbial Biotechnology
volume
15
issue
8
pages
2176 - 2190
publisher
John Wiley & Sons Inc.
external identifiers
  • pmid:35349220
  • scopus:85127247036
ISSN
1751-7907
DOI
10.1111/1751-7915.14052
project
STEPS – Sustainable Plastics and Transition Pathways, Phase 2
language
English
LU publication?
yes
additional info
Publisher Copyright: © 2022 The Authors. Microbial Biotechnology published by Society for Applied Microbiology and John Wiley & Sons Ltd.
id
3fd50f88-885e-4597-a651-3ab51a4a269c
date added to LUP
2022-04-20 17:32:56
date last changed
2024-11-05 00:36:19
@article{3fd50f88-885e-4597-a651-3ab51a4a269c,
  abstract     = {{<p>Bio-based 5-hydroxymethylfurfural (HMF) serves as an important platform for several chemicals, among which 2,5-furan dicarboxylic acid (FDCA) has attracted considerable interest as a monomer for the production of polyethylene furanoate (PEF), a potential alternative for fossil-based polyethylene terephthalate (PET). This study is based on the HMF oxidizing activity shown by <i>Mycobacterium </i>sp. MS 1601 cells and investigation of the enzyme catalysing the oxidation. The <i>Mycobacterium </i>whole cells oxidized the HMF to FDCA (60% yield) and hydroxymethyl furan carboxylic acid (HMFCA). A gene encoding a novel bacterial aryl alcohol oxidase, hereinafter MycspAAO, was identified in the genome and was cloned and expressed in <i>Escherichia coli</i> Bl21 (DE3). The purified MycspAAO displayed activity against several alcohols and aldehydes; 3,5 dimethoxy benzyl alcohol (veratryl alcohol) was the best substrate among those tested followed by HMF. 5-Hydroxymethylfurfural was converted to 5-formyl-2-furoic acid (FFCA) via diformyl furan (DFF) with optimal activity at pH 8 and 30–40°C. FDCA formation was observed during long reaction time with low HMF concentration. Mutagenesis of several amino acids shaping the active site and evaluation of the variants showed Y444F to have around 3-fold higher k<sub>cat</sub>/K<sub>m</sub> and ~1.7-fold lower K<sub>m</sub> with HMF.</p>}},
  author       = {{Sayed, Mahmoud and Gaber, Yasser and Junghus, Fredrik and Martín, Eric Valdés and Pyo, Sang-Hyun and Hatti-Kaul, Rajni}},
  issn         = {{1751-7907}},
  language     = {{eng}},
  number       = {{8}},
  pages        = {{2176--2190}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Microbial Biotechnology}},
  title        = {{Oxidation of 5-hydroxymethylfurfural with a novel aryl alcohol oxidase from <i>Mycobacterium </i>sp. MS1601}},
  url          = {{http://dx.doi.org/10.1111/1751-7915.14052}},
  doi          = {{10.1111/1751-7915.14052}},
  volume       = {{15}},
  year         = {{2022}},
}