Characterization of Paenibacillus sp. GKG Endo-β-1, 3-Glucanase, a Member of Family 81 Glycoside Hydrolases

Plakys, Gediminas; Gasparavičiūtė, Renata; Vaitekūnas, Justas; Rutkienė, Rasa; Meškys, Rolandas

doi:10.3390/microorganisms10101930

Cited by 7 publications

(2 citation statements)

References 40 publications

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“…Previously, we analysed the secretome of Paenibacillus sp. GKG grown on yeast CW as a sole carbon source [26] . Based on the LC–MS/MS proteomics data, several potential CAZymes were identified, among which “glycosyl hydrolase, family 30” from Paenibacillus pasadenensis (UniProt ID: A0A2N5N256) appeared as the nearest homolog, which was used to design the primers “Fw PsGly30A” and “Rv PsGly30A” (Table S1) and to clone the enzyme PsGly30A encoding gene from Paenibacillus sp.…”

Section: Resultsmentioning

confidence: 99%

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

Plakys,

Urbelienė,

Urbelis

et al. 2024

ChemBioChem

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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 has been used as a substrate. Therefore, PsGly30A is a promising catalyst for valorisation of the yeast‐related by‐products.

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Section: Resultsmentioning

confidence: 99%

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

Plakys,

Urbelienė,

Urbelis

et al. 2024

ChemBioChem

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“…These substances impart toughness and resistance to plant cell walls. Breaking the chemical bonds and structures within plant cell walls requires the involvement of multiple glycoside hydrolase (GH) families [14]. Currently, these enzyme activities are classified into 187 GH families based on their sequence and their functional and structural characteristics.…”

Section: Introductionmentioning

confidence: 99%

Exploring the Intestinal Microbial Community of Lantang Pigs through Metagenome-Assembled Genomes and Carbohydrate Degradation Genes

Yang,

Fan,

Jin

et al. 2024

Fermentation

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High-fiber, low-cost agricultural byproducts offer a sustainable alternative for mitigating the competition for crops between humans and livestock. Pigs predominantly utilize dietary fibers through the process of microbial fermentation within the gut. This study explored the gut microbiota and the capacity for carbohydrate degradation in 30 individual Lantang pigs, a breed indigenous to China. Through metagenomic analysis, a total of 671 metagenome-assembled genomes (MAGs) were assembled and assigned into 14 bacterial and 1 archaeal phylum, including 97 species from uncultured microbes. The phylum with the highest abundance were identified as Bacillota_A, Bacteroidota, and Bacillota. Remarkably, the investigation revealed nearly 10,000 genes implicated in the degradation of carbohydrates, with a pronounced prevalence within five principal bacterial genera: Prevotella, Cryptobacteroides, Gemmiger, Vescimonas, and Faecousia. Additionally, 87 distinct types of carbohydrate-degrading enzymes were exclusively identified within the gut microbiota of the Lantang pig. These insights not only enhance our understanding of the microbial diversity specific to native Chinese pig breeds but also augment the body of research regarding porcine fiber degradation capabilities. The implications of this study are twofold: it provides strategic directions for optimizing feed efficiency and reducing breeding costs, and it furnishes an expanded gene pool for the microbial synthesis of industrial enzymes in the future.

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Microbial β-glucanases: production, properties, and engineering

Wang

2023

World J Microbiol Biotechnol

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Characterization of Paenibacillus sp. GKG Endo-β-1, 3-Glucanase, a Member of Family 81 Glycoside Hydrolases

Cited by 7 publications

References 40 publications

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

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

Exploring the Intestinal Microbial Community of Lantang Pigs through Metagenome-Assembled Genomes and Carbohydrate Degradation Genes

Microbial β-glucanases: production, properties, and engineering

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