Purification and characterization of alginate lyase from marine Vibrio sp. YWA.
Extracellular alginate lyase secreted by marine Vibrio sp. YWA, isolated from decayed Laminaria japonica, was purified by a combination of ammonium sulfate precipitation and diethylaminoethyl-Sephacel column chromatography. The results show that the molecular mass of alginate lyase was approximately 62.5 kDa, with an optimal pH and temperature at pH 7.0 and 25 degrees C, respectively. K(m) was approximately 72.73 g/L. The activity of the enzyme was enhanced by EDTA and Zn(2+), but inhibited by Ba(2+). The substrates specificity analysis shows that it was specific for hydrolyzing poly-beta-D-1,4-mannuronate in alginate.
Wang
Yuan-Hong
YH
Marine Drug and Food Institute, Key Laboratory of Marine Drugs of Shandong Province, Key Laboratory of Marine Drugs, Ministry of Education, Ocean University of China, Qingdao 266003, China. yhwang@ouc.edu.cn
Yu
Guang-Li
GL
Wang
Xin-Min
XM
Lv
Zhi-Hua
ZH
Zhao
Xia
X
Wu
Zhi-Hong
ZH
Ji
Wei-Shang
WS
D004789:Enzyme Activation; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007795:Laminaria / Q000382:microbiology*; D011133:Polysaccharide-Lyases / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature; D014733:Vibrio / Q000201:enzymology*
D011133:Polysaccharide-Lyases; C016158:poly(beta-D-mannuronate) lyase