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
(2020) In Bioresource Technology 295.- 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,... (More)
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.
(Less)
- author
- Coconi Linares, Nancy ; Dilokpimol, Adiphol ; Stålbrand, Henrik LU ; Mäkelä, Miia R. and de Vries, Ronald P.
- organization
- publishing date
- 2020
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Galactomannan, Lignocellulosic biomass, Penicillium subrubescens, Pichia pastoris, Recombinant expression, α-Galactosidases
- in
- Bioresource Technology
- volume
- 295
- article number
- 122258
- publisher
- Elsevier
- external identifiers
-
- scopus:85073526359
- pmid:31639625
- ISSN
- 0960-8524
- DOI
- 10.1016/j.biortech.2019.122258
- language
- English
- LU publication?
- yes
- id
- 57029feb-282d-4159-9c45-9a14ee9b9ebe
- date added to LUP
- 2019-10-25 10:58:50
- date last changed
- 2024-05-14 23:51:42
@article{57029feb-282d-4159-9c45-9a14ee9b9ebe,
abstract = {{<p>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.</p>}},
author = {{Coconi Linares, Nancy and Dilokpimol, Adiphol and Stålbrand, Henrik and Mäkelä, Miia R. and de Vries, Ronald P.}},
issn = {{0960-8524}},
keywords = {{Galactomannan; Lignocellulosic biomass; Penicillium subrubescens; Pichia pastoris; Recombinant expression; α-Galactosidases}},
language = {{eng}},
publisher = {{Elsevier}},
series = {{Bioresource Technology}},
title = {{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}},
url = {{http://dx.doi.org/10.1016/j.biortech.2019.122258}},
doi = {{10.1016/j.biortech.2019.122258}},
volume = {{295}},
year = {{2020}},
}