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Abstract A truncated β-agarase gene without the Carbohydrate-binding Modules (Aga16A-△CBM) from a marine bacterium Microbulbifer sp. BH-1 was cloned and successfully expressed in Escherichia coli. It encoded 279 amino acid… Click to show full abstract
Abstract A truncated β-agarase gene without the Carbohydrate-binding Modules (Aga16A-△CBM) from a marine bacterium Microbulbifer sp. BH-1 was cloned and successfully expressed in Escherichia coli. It encoded 279 amino acid (aa) with a predicted molecular mass of 42.1 kDa. The recombinant β-agarase (Aga16A-△CBM) showed the highest sequence identity of 49% with the glycoside hydrolase (GH) family 16 β-agarases AgaA and AgaB from Zobellia galactanivorans. Aga16A-△CBM showed optimal activity at 55°C and pH 8.0, respectively. It was stable within the pH range of 5.0–9.5 and up to 50°C. Km and Vmax values of Aga16A-△CBM for agarose were 1.32 mg ml−1 and 860.9 μmol min−1mg−1, respectively. In additional, agarose was hydrolyzed by Aga16A-△CBM to produce 18.4 mg mL−1 neoagarotetraose with the high yield of 93.2% (w/w). These desirable properties of Aga16A-△CBM may make it attractive in neoagarotetraose production.
Journal Title: Process Biochemistry
Year Published: 2019
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