Abstract
Τhe β-agarase gene agaA, cloned from a marine bacterium, Pseudoalteromonas sp. CY24, consists of 1,359 nucleotides encoding 453 amino acids in a sequence corresponding to a catalytic domain of glycosyl hydrolase family 16 (GH16) and a carbohydrate-binding module type 13 (CBM13). The recombinant enzyme is an endo-type agarase that hydrolyzes β-1,4-linkages of agarose, yielding neoagarotetraose and neoagarohexaose as the predominant products. In two cleavage patterns, AgaA digested the smallest substrate, neoagarooctaose, into neoagarobiose, neoagarotetraose and neoagarohexaose. Site directed mutation was performed to investigate the differences between AgaA and AgaD of Vibrio sp. PO-303, identifying residues V109VTS112 as playing a key role in the enzyme reaction.
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This work was supported by the Key Project of Chinese National Programs for High Technology Research and Development (NO. 2007AA091506).
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Lu, X., Chu, Y., Wu, Q. et al. Cloning, expression and characterization of a new agarase-encoding gene from marine Pseudoalteromonas sp.. Biotechnol Lett 31, 1565–1570 (2009). https://doi.org/10.1007/s10529-009-0042-1
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DOI: https://doi.org/10.1007/s10529-009-0042-1