Conversion of β-1,6-glucans to gentiobiose using an endo-β-1,6-glucanase PsGly30A from Paenibacillus sp. GKG

Chembiochem. 2024 Mar 5:e202400010. doi: 10.1002/cbic.202400010. Online ahead of print.ABSTRACTA 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 has been used as a substrate. Therefore, PsGly30A is a promising catalyst for valorisation of the yeast-related by-products.PMID:38439711 | DOI:10.1002/cbic.202400010
Source: Chembiochem - Category: Biochemistry Authors: Source Type: research