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Molecular cloning, characterization and enzymatic properties of a novel βeta-agarase from a marine isolate Psudoalteromonas sp. AG52 BJM
Oh,Chulhong; Nikapitiya,Chamilani; Lee,Youngdeuk; Whang,Ilson; Kang,Do-Hyung; Heo,Soo-Jin; Choi,Young-Ung; Lee,Jehee.
An agar-degrading Pseudoalteromonas sp. AG52 bacterial strain was identified from the red seaweed Gelidium amansii collected from Jeju Island, Korea. A β-agarase gene which has 96.8% nucleotide identity to Aeromonas β-agarase was cloned from this strain, and was designated as agaA. The coding region is 870 bp, encoding 290 amino acids and possesses characteristic features of the glycoside hydrolase family (GHF)-16. The predicted molecular mass of the mature protein was 32 kDa. The recombinant β-agarase (rAgaA) was overexpressed in Escherichia coli and purified as a fusion protein. The optimal temperature and pH for activity were 55 ºC and 5.5, respectively. The enzyme had a specific activity of 105.1 and 79.5 unit/mg toward agar and agarose, respectively....
Tipo: Info:eu-repo/semantics/article Palavras-chave: Agar; Aeromonas sp; Β-agarase; Pseudoalteromonas sp; GHF-16; Neoagaro-oligosaccharides.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822010000400006
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