Comparative characterization of nine novel GH51, GH54 and GH62 α‐<scp>l</scp>‐arabinofuranosidases from <i>Penicillium subrubescens</i>

Linares, Nancy; Li, Xinxin; Dilokpimol, Adiphol

doi:10.1002/1873-3468.14278

Cited by 11 publications

(5 citation statements)

References 37 publications

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“…However, using 10 mM as the highest p NPA concentration and enzyme concentrations of 0.036 µM it can be concluded that the Michaelis Menten constant K m must at least be higher than the substrate concentration of 10 mM ( Li 2017 ). This and the values obtained using p NPG as a substrate (4.2–8.5 mM), were higher than most of the reported K m values for Abf, which range from about 0.1 to 1.5 mM p NPA ( Inacio et al, 2008 ; Matsuzawa et al, 2017 ; Coconi Linares et al, 2022 ).…”

Section: Discussioncontrasting

confidence: 70%

Biochemical and Structural Characterization of Thermostable GH159 Glycoside Hydrolases Exhibiting α-L-Arabinofuranosidase Activity

Baudrexl

Fida

Berk

et al. 2022

Front. Mol. Biosci.

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Functional, biochemical, and preliminary structural properties are reported for three glycoside hydrolases of the recently described glycoside hydrolase (GH) family 159. The genes were cloned from the genomic sequences of different Caldicellulosiruptor strains. This study extends the spectrum of functions of GH159 enzymes. The only activity previously reported for GH159 was hydrolytic activity on β-galactofuranosides. Activity screening using a set of para-nitrophenyl (pNP) glycosides suggested additional arabinosidase activity on substrates with arabinosyl residues, which has not been previously reported for members of GH159. Even though the thermophilic enzymes investigated—Cs_Gaf159A, Ch_Gaf159A, and Ck_Gaf159A—cleaved pNP-α-l-arabinofuranoside, they were only weakly active on arabinogalactan, and they did not cleave arabinose from arabinan, arabinoxylan, or gum arabic. However, the enzymes were able to hydrolyze the α-1,3-linkage in different arabinoxylan-derived oligosaccharides (AXOS) with arabinosylated xylose at the non-reducing end (A3X, A2,3XX), suggesting their role in the intracellular hydrolysis of oligosaccharides. Crystallization and structural analysis of the apo form of one of the Caldicellulosiruptor enzymes, Ch_Gaf159A, enabled the elucidation of the first 3D structure of a GH159 member. This work revealed a five-bladed β-propeller structure for GH159 enzymes. The 3D structure and its substrate-binding pocket also provides an explanation at the molecular level for the observed exo-activity of the enzyme. Furthermore, the structural data enabled the prediction of the catalytic amino acids. This was supported by the complete inactivation by mutation of residues D19, D142, and E190 of Ch_Gaf159A.

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Section: Discussioncontrasting

confidence: 70%

Biochemical and Structural Characterization of Thermostable GH159 Glycoside Hydrolases Exhibiting α-L-Arabinofuranosidase Activity

Baudrexl

Fida

Berk

et al. 2022

Front. Mol. Biosci.

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“…GH51 α-L-arabinofuranosidases from Penicillium subrubescens and Pleurotus ostreatus had an optimal temperature range of 40 50 °C and an optimal pH range of 4.0. 17) 18) Gt Abf51A demonstrated greater activity on the more acidic side than the enzymes of previous reports. Gt Abf51A had nearly the same thermal stability as α-L-arabinofuranosidase from P. subrubescens , and was more stable in the acidic pH range of 2.2 to 4.0.…”

Section: Resultscontrasting

confidence: 53%

Characterization of an α-L-Arabinofuranosidase GH51 from the Brown-rot Fungus <i>Gloeophyllum trabeum</i>

2023

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GtAbf51A, in contrast, efficiently hydrolyzed arabinoxylooligosaccharides, particularly O-α-L-arabinofuranosyl-(1→3)-O-β-D-xylopyranosyl-(1→4)-β-Dxylopyranose, which is the principal product of GH10 β-xylanase. These data suggest that GtAbf51A cooperates with other xylan-degrading enzymes, such as β-xylanase, to degrade xylan in nature. α-L-arabinofuranosidase, brown-rot fungi, glycoside hydrolase family 51, Gloeophyllum trabeum, hemicellulose, wood rotting fungi

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“…However, high variability was also observed in the number of genes within the same phyla. For example, multiple gene copies of GH51-, GH54-, and GH62-encoding ABFs were identified in P. subrubescens, which implies a potential enhancement in the ability of P. subrubescens to release L-arabinose from plant biomass in a more specific manner [ 68 ]. Moreover, this is in line with our finding that CAZy genes involved in xylan, pectin, and xyloglucan in P. subrubescens show evident L-arabinose specificity ( Figure 3 C).…”

Section: Discussionmentioning

confidence: 99%

Comparative Genomics and Transcriptomics Analyses Reveal Divergent Plant Biomass-Degrading Strategies in Fungi

Li,

Wiebenga,

Lipzen

et al. 2023

JoF

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Plant biomass is one of the most abundant renewable carbon sources, which holds great potential for replacing current fossil-based production of fuels and chemicals. In nature, fungi can efficiently degrade plant polysaccharides by secreting a broad range of carbohydrate-active enzymes (CAZymes), such as cellulases, hemicellulases, and pectinases. Due to the crucial role of plant biomass-degrading (PBD) CAZymes in fungal growth and related biotechnology applications, investigation of their genomic diversity and transcriptional dynamics has attracted increasing attention. In this project, we systematically compared the genome content of PBD CAZymes in six taxonomically distant species, Aspergillus niger, Aspergillus nidulans, Penicillium subrubescens, Trichoderma reesei, Phanerochaete chrysosporium, and Dichomitus squalens, as well as their transcriptome profiles during growth on nine monosaccharides. Considerable genomic variation and remarkable transcriptomic diversity of CAZymes were identified, implying the preferred carbon source of these fungi and their different methods of transcription regulation. In addition, the specific carbon utilization ability inferred from genomics and transcriptomics was compared with fungal growth profiles on corresponding sugars, to improve our understanding of the conversion process. This study enhances our understanding of genomic and transcriptomic diversity of fungal plant polysaccharide-degrading enzymes and provides new insights into designing enzyme mixtures and metabolic engineering of fungi for related industrial applications.

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Comparative characterization of nine novel GH51, GH54 and GH62 α‐l‐arabinofuranosidases from Penicillium subrubescens

Cited by 11 publications

References 37 publications

Biochemical and Structural Characterization of Thermostable GH159 Glycoside Hydrolases Exhibiting α-L-Arabinofuranosidase Activity

Biochemical and Structural Characterization of Thermostable GH159 Glycoside Hydrolases Exhibiting α-L-Arabinofuranosidase Activity

Characterization of an α-L-Arabinofuranosidase GH51 from the Brown-rot Fungus <i>Gloeophyllum trabeum</i>

Comparative Genomics and Transcriptomics Analyses Reveal Divergent Plant Biomass-Degrading Strategies in Fungi

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