ArticleInternational journal of molecular sciences2016
Isolation and Characterization of a Glycosyl Hydrolase Family 16 β-Agarase from a Mangrove Soil Metagenomic Library.
Article in International journal of molecular sciences, 2016. 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.
- Prospecting Microbial Genomes for Biomolecules and Their Applications.Indian journal of microbiology · 2022Review
- What lies on macroalgal surface: diversity of polysaccharide degraders in culturable epiphytic bacteria.AMB Express · 2022Article
- Recent Advances in Function-based Metagenomic Screening.Genomics, proteomics & bioinformatics · 2018Review
- Biotechnology Potential of Marine Fungi Degrading Plant and Algae Polymeric Substrates.Frontiers in microbiology · 2018Review
- Metagenomics Investigation of Agarlytic Genes and Genomes in Mangrove Sediments in China: A Potential Repertory for Carbohydrate-Active Enzymes.Frontiers in microbiology · 2018Article
- Extracellular expression of a novel β-agarase from Microbulbifer sp. Q7, isolated from the gut of sea cucumber.AMB Express · 2017Article
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Authors and funding
3 authors.
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Abstract
A mangrove soil metagenomic library was constructed and a β-agarase gene designated as AgaML was isolated by functional screening. The gene encoded for a 659-amino-acids polypeptide with an estimated molecular mass of 71.6 kDa. The deduced polypeptide sequences of AgaML showed the highest identity of 73% with the glycoside hydrolase family 16 β-agarase from Microbulbifer agarilyticus in the GenBank database. AgaML was cloned and highly expressed in Escherichia coli BL21(DE3). The purified recombinant protein, AgaML, showed optimal activity at 50 °C and pH 7.0. The kinetic parameters of Km and Vmax values toward agarose were 4.6 mg·mL(-1) and 967.5 μM·min(-1)·mg(-1), respectively. AgaML hydrolyzed the β-1,4-glycosidic linkages of agar to generate neoagarotetraose (NA4) and neoagarohexaose (NA6) as the main products. These characteristics suggest that AgaML has potential application in cosmetic, pharmaceuticals and food industries.
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