A C1/C4-Oxidizing AA10 Lytic Polysaccharide Monooxygenase from Paenibacillus xylaniclasticus Strain TW1
- Authors
- Type
- Published Article
- Journal
- Journal of Applied Glycoscience
- Publisher
- The Japanese Society of Applied Glycoscience
- Publication Date
- Mar 03, 2023
- Volume
- 70
- Issue
- 1
- Pages
- 39–42
- Identifiers
- DOI: 10.5458/jag.jag.JAG-2022_0011
- PMID: 37033115
- PMCID: PMC10074029
- Source
- PubMed Central
- Keywords
- Disciplines
- License
- Unknown
Abstract
Lytic polysaccharide monooxygenases (LPMO) are key enzymes for the efficient degradation of lignocellulose biomass with cellulases. A lignocellulose-degradative strain, Paenibacillus xylaniclasticus TW1, has LPMO-encoding Px AA10A gene. Neither the C1/C4-oxidizing selectivity nor the enzyme activity of Px AA10A has ever been characterized. In this study, the C1/C4-oxidizing selectivity of Px AA10A and the boosting effect for cellulose degradation with a cellulase cocktail were investigated. The full-length Px AA10A (r Px AA10A) and the catalytic domain (r Px AA10A-CD) were heterologously expressed in Escherichia coli and purified. To identify the C1/C4-oxidizing selectivity of Px AA10A, cellohexaose was used as a substrate with the use of r Px AA10A-CD, and the products were analyzed by MALDI-TOF/MS. As a result, aldonic acid cellotetraose and cellotetraose, the products from C1-oxidization and C4-oxidization, respectively, were detected. These results indicate that Px AA10A is a C1/C4-oxidizing LPMO. It was also found that the addition of r Px AA10A into a cellulase cocktail enhanced the cellulose-degradation efficiency.
