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

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Abstract

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.

Detaljer

Författare
  • Nancy Coconi Linares
  • Adiphol Dilokpimol
  • Henrik Stålbrand
  • Miia R. Mäkelä
  • Ronald P. de Vries
Enheter & grupper
Externa organisationer
  • Utrecht University
  • University of Helsinki
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Biokatalys och enzymteknik

Nyckelord

Originalspråkengelska
Artikelnummer122258
TidskriftBioresource Technology
Volym295
StatusPublished - 2020
PublikationskategoriForskning
Peer review utfördJa