Characterization of A Neoagarobiose-Producing and Thermostable β-agarase from Agarivorans sp. AL1 and Antioxidant Activity of the Enzymatic Hydrolysates
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Abstract:
The agarase gene AL1 was amplified by PCR and cloned into pET-28a expression vector. The expression product was purified by affinity chromatography to study the enzymatic properties of the recombinant enzyme. The enzymatic hydrolysate was identified by TLC and LC-MS, and its reducing ability and scavenging ability of DPPH, ABTS+· and ·OH radicals were determined, and the antioxidant activity of the hydrolysate was analyzed. The molecular weight of the recombinant agarase from Agarivorans sp. AL1 was 105 ku. The agarase could specifically degrade agar as a β-agarase. The recombinant agarase showed the maximum activity at 50 ℃ and pH 7.00. The recombinant agarase was stable in a wide pH range from 5.00 to 11.00 below 50 ℃, indicating that the recombinant enzyme had good thermal stability and pH stability. The enzymatic hydrolysate product was identified as neoagarobiose by TLC and LC-MS. The enzymatic hydrolysates had the reducing power. The half-inhibition concentration IC50 of the enzymatic hydrolysate to ·OH, ABTS and DPPH free radicals are 1.28 mg/mL, 3.46 mg/mL and 9.87 mg/mL, respectively, indicating that the hydrolysate had good antioxidant activity.
