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Background  The development of sustainable technologies for plant cell wall degradation greatly depends on enzymes with hydrolytic activities against carbohydrates. The waste by-products of agricultural cereals are important biomass sources because they contain large amounts of saccharides. Achieving efficient debranching and depolymerization are two important objectives for increasing the utilization of such renewable bioresources. GH51 α- l -arabinofuranosidases are important in biomass pretreatment because they act synergistically with other enzymes during hemicellulose hydrolysis.    Results  A GH51 α- l -arabinofuranosidase from  Talaromyces leycettanus  JCM12802 was heterologously expressed in  Pichia pastoris  GS115 and characterized. The recombinant α- l -arabinofuranosidase,  Tl Abf51, showed an optimum temperature and pH of 55–60 °C and 3.5–4.0, respectively, and remained stable at 50 °C and pH 3.0–9.0.  Tl Abf51 showed a higher catalytic efficiency (5712 mM −1  s −1 ) than most fungal α- l -arabinofuranosidases towards the substrate 4-nitrophenyl-α- l -arabinofuranoside. Moreover,  Tl Abf51 preferentially removed 1,2- or 1,3-linked arabinofuranose residues from arabinoxylan and acted synergistically with the bifunctional xylanase/cellulase  Tc Xyn10A at an activity ratio of 5:1. The highest yields of arabinose and xylooligosaccharides were obtained when  Tl Abf51 was added after  Tc Xyn10A or when both enzymes were added simultaneously. High-performance anion-exchange chromatography analyses showed that (i) arabinose and xylooligosaccharides with low degrees of polymerization (DP1–DP5) and (ii) arabinose and xylooligosaccharides (DP1–DP3) were the major hydrolysates obtained during the hydrolysis of sodium hydroxide-pretreated cornstalk and corn bran, respectively.    Conclusions  In contrast to other fungal GH51 α- l -arabinofuranosidases, recombinant  Tl Abf51 showed excellent stability over a broad pH range and high catalytic efficiency. Moreover,  Tl Abf51 acted synergistically with another hemicellulase to digest arabino-polysaccharides. These favorable enzymatic properties make  Tl Abf51 attractive for biomass pretreatment and biofuel production.    Electronic supplementary material  The online version of this article (10.1186/s12934-019-1192-z) contains supplementary material, which is available to authorized users.

A GH51 α-l-arabinofuranosidase from Talaromyces leycettanus strain JCM12802 that selectively drives synergistic lignocellulose hydrolysis