ArticleAMB Express2018
Molecular cloning, expression, and functional characterization of the β-agarase AgaB-4 from Paenibacillus agarexedens.
Article in AMB Express, 2018. 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, 18 citations in OpenAlex.
- Odd-Numbered Agaro-Oligosaccharides Produced by α-Neoagaro-Oligosaccharide Hydrolase Exert Antioxidant Activity in Human Dermal Fibroblasts.Marine drugs · 2024Article
- Biochemical characterization of Fsa16295Glu fromFrontiers in microbiology · 2024Article
- Extracellular production of a thermostable Cellvibrio endolytic β-agarase in Escherichia coli for agarose liquefaction.AMB Express · 2023Article
- Characterization and Modeling of Thermostable GH50 Agarases from Microbulbifer elongatus PORT2.Marine biotechnology (New York, N.Y.) · 2021Article
- Enzymatic characterization of a novel recombinant 1,3-α-3,6-anhydro-L-galactosidase specific for neoagarobiose hydrolysis into monosaccharides.Applied microbiology and biotechnology · 2021Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
In this study, a β-agarase gene, agaB-4, was isolated for the first time from the agar-degrading bacterium Paenibacillus agarexedens BCRC 17346 by using next-generation sequencing. agaB-4 consists of 2652 bp and encodes an 883-amino acid protein with an 18-amino acid signal peptide. agaB-4 without the signal peptide DNA was cloned and expressed in Escherichia coli BL21(DE3). His-tagged recombinant AgaB-4 (rAgaB-4) was purified from the soluble fraction of E. coli cell lysate through immobilized metal ion affinity chromatography. The optimal temperature and pH of rAgaB-4 were 55 °C and 6.0, respectively. The results of a substrate specificity test showed that rAgaB-4 could degrade agar, high-melting point agarose, and low-melting point agarose. The V
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