Oxidation of 5‐hydroxymethylfurfural with a novel aryl alcohol oxidase from Mycobacterium sp. MS1601
Summary 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 polyethy...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2022-08-01
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| Series: | Microbial Biotechnology |
| Online Access: | https://doi.org/10.1111/1751-7915.14052 |
| _version_ | 1818041686710812672 |
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| author | Mahmoud Sayed Yasser Gaber Fredrik Junghus Eric Valdés Martín Sang‐Hyun Pyo Rajni Hatti‐Kaul |
| author_facet | Mahmoud Sayed Yasser Gaber Fredrik Junghus Eric Valdés Martín Sang‐Hyun Pyo Rajni Hatti‐Kaul |
| author_sort | Mahmoud Sayed |
| collection | DOAJ |
| description | Summary 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. |
| first_indexed | 2024-12-10T08:34:22Z |
| format | Article |
| id | doaj.art-29682f7ecddf4898a19465ea2c4b7d76 |
| institution | Directory Open Access Journal |
| issn | 1751-7915 |
| language | English |
| last_indexed | 2024-12-10T08:34:22Z |
| publishDate | 2022-08-01 |
| publisher | Wiley |
| record_format | Article |
| series | Microbial Biotechnology |
| spelling | doaj.art-29682f7ecddf4898a19465ea2c4b7d762022-12-22T01:56:01ZengWileyMicrobial Biotechnology1751-79152022-08-011582176219010.1111/1751-7915.14052Oxidation of 5‐hydroxymethylfurfural with a novel aryl alcohol oxidase from Mycobacterium sp. MS1601Mahmoud Sayed0Yasser Gaber1Fredrik Junghus2Eric Valdés Martín3Sang‐Hyun Pyo4Rajni Hatti‐Kaul5Division of Biotechnology Department of Chemistry Center for Chemistry and Chemical Engineering Lund University Lund SE‐22100 SwedenDepartment of Microbiology and Immunology Faculty of Pharmacy Beni‐Suef University Beni‐Suef 62511 EgyptDivision of Biotechnology Department of Chemistry Center for Chemistry and Chemical Engineering Lund University Lund SE‐22100 SwedenDivision of Biotechnology Department of Chemistry Center for Chemistry and Chemical Engineering Lund University Lund SE‐22100 SwedenDivision of Biotechnology Department of Chemistry Center for Chemistry and Chemical Engineering Lund University Lund SE‐22100 SwedenDivision of Biotechnology Department of Chemistry Center for Chemistry and Chemical Engineering Lund University Lund SE‐22100 SwedenSummary 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.https://doi.org/10.1111/1751-7915.14052 |
| spellingShingle | Mahmoud Sayed Yasser Gaber Fredrik Junghus Eric Valdés Martín Sang‐Hyun Pyo Rajni Hatti‐Kaul Oxidation of 5‐hydroxymethylfurfural with a novel aryl alcohol oxidase from Mycobacterium sp. MS1601 Microbial Biotechnology |
| title | Oxidation of 5‐hydroxymethylfurfural with a novel aryl alcohol oxidase from Mycobacterium sp. MS1601 |
| title_full | Oxidation of 5‐hydroxymethylfurfural with a novel aryl alcohol oxidase from Mycobacterium sp. MS1601 |
| title_fullStr | Oxidation of 5‐hydroxymethylfurfural with a novel aryl alcohol oxidase from Mycobacterium sp. MS1601 |
| title_full_unstemmed | Oxidation of 5‐hydroxymethylfurfural with a novel aryl alcohol oxidase from Mycobacterium sp. MS1601 |
| title_short | Oxidation of 5‐hydroxymethylfurfural with a novel aryl alcohol oxidase from Mycobacterium sp. MS1601 |
| title_sort | oxidation of 5 hydroxymethylfurfural with a novel aryl alcohol oxidase from mycobacterium sp ms1601 |
| url | https://doi.org/10.1111/1751-7915.14052 |
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