ArticleApplied biochemistry and biotechnology2022
Cloning, Expression, and Characterization of Endo-β-1,6-galactanase PoGal30 from Penicillium oxalicum.
Article in Applied biochemistry and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 9 citations in OpenAlex.
- Expression and characterization of an endo-β-1,6-galactanase from Arabidopsis thaliana.The Biochemical journal · 2025Article
- β-galactanase: an effective tool for the degradation of plant β-ᴅ-galactan.World journal of microbiology & biotechnology · 2025Review
- Cloning and expression of theFrontiers in microbiology · 2025Article
- Insight into the phylogeny and metabolic divergence ofFrontiers in microbiology · 2023Article
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8 authors at 3 institutions in 1 country.
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Abstract
Because β-1,6-galactans are significant components in arabinogalactans from plant cell walls, identifying selective endo-β-1,6-galactanases is crucial to degrading these polysaccharides and to analyzing and modifying their structures. Here, we cloned and expressed in E. coli a novel endo-β-1,6-galactanase in the glycosidic hydrolase family 30 (GH30) from Penicillium oxalicum. Our recombinant PoGal30 hydrolase (1464 bp gene) that contains an N-terminal His-tag for purification by nickel affinity chromatography has a specific activity of 3.8 U/mg on the substrate de-arabinosylated gum Arabic (dGA) polysaccharide. The enzyme has 487 residues with a molecular mass of 60 kDa, an isoelectric point of 6, and functional pH and temperature optima of pH 2.5 to pH 5.0 and 40 °C, respectively. While the activity of PoGal30 is activated by Mg
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