Conversion of β-1,6-Glucans to Gentiobiose using an endo-β-1,6-Glucanase PsGly30A from Paenibacillus sp. GKG.

Autor: Plakys G; Department of Molecular Microbiology and Biotechnology, Institute of Biochemistry, Life Sciences Center, Vilnius University, Sauletekio 7, LT-10257, Vilnius, Lithuania.; Department of Research and Development Roquette Amilina, AB, J. Janonio 12, LT, 35101 Panevezys, Lithuania., Urbelienė N; Department of Molecular Microbiology and Biotechnology, Institute of Biochemistry, Life Sciences Center, Vilnius University, Sauletekio 7, LT-10257, Vilnius, Lithuania., Urbelis G; Department of Organic Chemistry, Center for Physical Sciences and Technology, Akademijos 7, LT-08412, Vilnius, Lithuania., Vaitekūnas J; Department of Molecular Microbiology and Biotechnology, Institute of Biochemistry, Life Sciences Center, Vilnius University, Sauletekio 7, LT-10257, Vilnius, Lithuania., Labanauskas L; Department of Organic Chemistry, Center for Physical Sciences and Technology, Akademijos 7, LT-08412, Vilnius, Lithuania., Mažonienė E; Department of Research and Development Roquette Amilina, AB, J. Janonio 12, LT, 35101 Panevezys, Lithuania., Meškys R; Department of Molecular Microbiology and Biotechnology, Institute of Biochemistry, Life Sciences Center, Vilnius University, Sauletekio 7, LT-10257, Vilnius, Lithuania.
Jazyk: angličtina
Zdroj: Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Apr 16; Vol. 25 (8), pp. e202400010. Date of Electronic Publication: 2024 Mar 21.
DOI: 10.1002/cbic.202400010
Abstrakt: A plethora of di- and oligosaccharides isolated from the natural sources are used in food and pharmaceutical industry. An enzymatic hydrolysis of fungal cell wall β-glucans is a good alternative to produce the desired oligosaccharides with different functionalities, such as the flavour enhancer gentiobiose. We have previously identified PsGly30A as a potential yeast cell wall degrading β-1,6-glycosidase. The aim of this study is to characterise the PsGly30A enzyme, a member of the GH30 family, and to evaluate its suitability for the production of gentiobiose from β-1,6-glucans. An endo-β-1,6-glucanase PsGly30A encoding gene from Paenibacillus sp. GKG has been cloned and overexpressed in Escherichia coli. The recombinant enzyme has been active towards pustulan and yeast β-glucan, but not on laminarin from the Laminaria digitata, confirming the endo-β-1,6-glucanase mode of action. The PsGly30A shows the highest activity at pH 5.5 and 50 °C. The specific activity of PsGly30A on pustulan (1262±82 U/mg) is among the highest reported for GH30 β-1,6-glycosidases. Moreover, gentiobiose is the major reaction product when pustulan, yeast β-glucan or yeast cell walls have been used as a substrate. Therefore, PsGly30A is a promising catalyst for valorisation of the yeast-related by-products.
(© 2024 Wiley‐VCH GmbH.)
Databáze: MEDLINE
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