ArticleApplied microbiology and biotechnology2021
Heterologous expression and characterization of a novel glycoside hydrolase family 55 β-1,3-glucanase, AcGluA, from Archangium sp. strain AC19.
Article in Applied microbiology and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Precision hydrolysis: tailored yeast processing enzymes for yeast-based products.Applied microbiology and biotechnology · 2026Review
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- Cloning and expression of theFrontiers in microbiology · 2025Article
- Microbial β-glucanases: production, properties, and engineering.World journal of microbiology & biotechnology · 2023Review
- Engineering Caldicellulosiruptor bescii with Surface Layer Homology Domain-Linked Glycoside Hydrolases Improves Plant Biomass Solubilization.Applied and environmental microbiology · 2022Article
- Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update for 2021-2022.Mass spectrometry reviewsReview
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Some microbial-associated molecular patterns (MAMPs), like glucan oligosaccharides, can be recognized by pattern recognition receptors (PRRs) of plant to elicit further immunity response. In this study, a novel glycoside hydrolase family 55 β-1,3-glucanase (AcGluA) from Archangium sp. strain AC19 was cloned and expressed in Escherichia coli. Among the reported β-1, 3-glucanases from the glycoside hydrolase 55 family, the purified AcGluA exhibited the highest activity on laminarin at pH 6.0 and 60 °C with 112.3 U/mg. Activity of AcGluA was stable in the range of pH 4.0-9.0 and at temperatures below 60 °C. The K
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