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Comparative characterization of nine novel GH51, GH54 and GH62 α‐ l ‐arabinofuranosidases from Penicillium subrubescens
Author(s) -
Coconi Linares Nancy,
Li Xinxin,
Dilokpimol Adiphol,
Vries Ronald P.
Publication year - 2022
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.14278
Subject(s) - fungus , penicillium , enzyme , biomass (ecology) , arabinose , glycoside hydrolase , botany , diversification (marketing strategy) , chemistry , biochemistry , gene , food science , biology , fermentation , ecology , marketing , business , xylose
α‐ l ‐Arabinofuranosidases (ABFs) are important enzymes in plant biomass degradation with a wide range of applications. The ascomycete fungus Penicillium subrubescens has more α‐ l ‐arabinofuranosidase‐encoding genes in its genome compared to other Penicillia. We characterized nine ABFs from glycoside hydrolase (GH) families GH51, GH54 and GH62 from this fungus and demonstrated that they have highly diverse specificity and activity levels, indicating that the expansion was accompanied by diversification of the enzymes. Comparison of the substrate preference of the enzymes to the expression of the corresponding genes when the fungus was grown on either of two plant biomass substrates did not show a clear correlation, suggesting a more complex regulatory system governing l ‐arabinose release from plant biomass by P. subrubescens .