Recombinant production and characterization of six novel GH27 and GH36 α-galactosidases from Penicillium subrubescens and their synergism with a commercial mannanase during the hydrolysis of lignocellulosic biomass

Research output: Contribution to journalArticle


α-Galactosidases are important industrial enzymes for hemicellulosic biomass degradation or modification. In this study, six novel extracellular α-galactosidases from Penicillium subrubescens were produced in Pichia pastoris and characterized. All α-galactosidases exhibited high affinity to pNPαGal, and only AglE was not active towards galacto-oligomers. Especially AglB and AglD released high amounts of galactose from guar gum, carob galactomannan and locust bean, but combining α-galactosidases with an endomannanase dramatically improved galactose release. Structural comparisons to other α-galactosidases and homology modelling showed high sequence similarities, albeit significant differences in mechanisms of productive binding, including discrimination between various galactosides. To our knowledge, this is the first study of such an extensive repertoire of extracellular fungal α-galactosidases, to demonstrate their potential for degradation of galactomannan-rich biomass. These findings contribute to understanding the differences within glycoside hydrolase families, to facilitate the development of new strategies to generate tailor-made enzymes for new industrial bioprocesses.


  • Nancy Coconi Linares
  • Adiphol Dilokpimol
  • Henrik Stålbrand
  • Miia R. Mäkelä
  • Ronald P. de Vries
External organisations
  • Utrecht University
  • University of Helsinki
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biocatalysis and Enzyme Technology


  • Galactomannan, Lignocellulosic biomass, Penicillium subrubescens, Pichia pastoris, Recombinant expression, α-Galactosidases
Original languageEnglish
Article number122258
JournalBioresource Technology
Publication statusPublished - 2020
Publication categoryResearch