Cloning, expression and characterization of a new agarase-encoding gene from marine Pseudoalteromonas sp.

被引：25

作者：

Lu, Xinzhi ^{[1
]}

Chu, Yan ^{[1
]}

Wu, Qianqian ^{[1
]}

Gu, Yuchao ^{[1
]}

Han, Feng ^{[1
]}

Yu, Wengong ^{[1
]}

机构：

[1] Ocean Univ China, Dept Mol Biol, Sch Med & Pharm, Qingdao 266003, Peoples R China

来源：

BIOTECHNOLOGY LETTERS | 2009年 / 31卷 / 10期

关键词：

beta-Agarase; Carbohydrate binding module; Glycoside hydrolase; Neoagaro-oligosaccharide; Pseudoalteromonas sp CY24; SP STRAIN PO-303; BETA-AGARASE; MOLECULAR-CLONING; BACTERIUM; OLIGOSACCHARIDES; MUTAGENESIS; ENZYMES; BINDING; SUGAR; AGAB;

D O I：

10.1007/s10529-009-0042-1

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Icurrency signhe beta-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 beta-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.

引用

页码：1565 / 1570

页数：6

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