ArticleAMB Express2017
Extracellular expression of a novel β-agarase from Microbulbifer sp. Q7, isolated from the gut of sea cucumber.
Article in AMB Express, 2017. 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, 27 citations in OpenAlex.
- Polymer degrading marineBeilstein journal of organic chemistry · 2024Review
- Marine microbial enzymes for the production of algal oligosaccharides and its bioactive potential for application as nutritional supplements.Folia microbiologica · 2022Review
- Enzymatic Preparation of Low-Molecular-WeightFrontiers in bioengineering and biotechnology · 2021Article
- Complete Genome Sequence of Cellulase-ProducingMicrobiology resource announcements · 2020Article
- Evaluation of Prebiotic Potential of Three Marine Algae Oligosaccharides from Enzymatic Hydrolysis.Marine drugs · 2019Article
- Recombinant β-agarases: insights into molecular, biochemical, and physiochemical characteristics.3 Biotech · 2018Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
A novel endo-type β-agarase was cloned from an agar-degrading bacterium, Microbulbifer sp. Q7 (CGMCC No. 14061), that was isolated from sea cucumber gut. The agarase-encoding gene, ID2563, consisted of 1800 bp that encoded a 599-residue protein with a signal peptide of 19 amino acids. Sequence analysis suggested that the agarase belongs to the GH16 family. The agarase was expressed in Escherichia coli with a total activity of 4.99 U/mL in fermentation medium. The extracellular enzyme activity accounted for 65.73% of the total activity, which indicated that the agarase can be extracellularly secreted using the wild-type signal peptide from Microbulbifer sp. Q7. The agarase exhibited maximal activity at approximately 40 °C and pH 6.0. It was stable between pH 6.0 and pH 9.0, which was a much wider range than most of the reported agarases. The agarase was sensitive to some metal ions (Cu
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