Cloning, Expression, and Characterization of a Novel GH-16 β-Agarase from Agarivorans sp. JA-1

Abstract

Authors report the glycoside hydrolase (GH) family 16 β-agarase from the strain of Agarivorans sp.JA-1, which authors previously stated as recombinant expression and characterization of GH-50 and GH-118 β-agarase. It comprised an open reading frame of 1,362 base pairs, which encodes a protein of 49,830 daltons consisting of 453 amino acid residues. Valuation of the total sequence showed that the enzyme has 98% nucleotide and 99% amino acid sequence similarities to those of GH-16 β-agarase from Pseudoalteromonas sp. CY24. The gene corresponding to a mature protein of 429 amino acids was recombinantly expressed in Escherichia coli, and the enzyme was purified to homogeneity by affinity chromatography. It showed maximal activity at 40°C and pH 5.0, representing 67.6 units/mg. Thin layer chromatography revealed that mainly neoagarohexaose and neoagarotetraose were produced from agarose. The enzyme would be valuable for the industrial production of functional neoagarooligosaccharides.

Characterization of Agarase Produced from the Isolated Marine Bacterium Marinomonas sp. SH-2

“…고부가가치 소재로서의 활용 가능성이 높은 한천올리고당 및 네오한천올리고당의 보고된 기능성은 면역증진, 항암작용, 간세포보호, 항산화작용, 항균작용, 미백작용, 보습효과 등이 고, 바이오에탄올 생산을 포함하는 많은 연구가 수행되어져 왔다 [3,11].…”