Two types of bacterial alginate lyases.
The extracellular alginate lyases were purified from Vibrio harveyi AL-128 and V. alginolyticus ATCC 17749. The former enzyme appears to be specific for alpha-1,4 bonds involving L-guluronate units in alginate, whereas the latter exhibits specificity for beta-1,4 bonds involving D-mannuronate units. The molecular weights of the enzymes were estimated to be 57,000 and 47,000, and they had isoelectric points of 4.3 and 4.6, respectively. The enzyme from strain AL-128 was most active at NaCl concentrations of 0.3 to 1.0 M. Optimum activity of the enzyme from strain ATCC 17749 was found in the presence of 5 to 10 mM CaCl2.
Kitamikado
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M
Department of Fisheries, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
Tseng
C H
CH
Yamaguchi
K
K
Nakamura
T
T
D000464:Alginates; D002122:Calcium Chloride; D020723:Glucuronic Acid; D006603:Hexuronic Acids; D007526:Isoelectric Point; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008970:Molecular Weight; D011133:Polysaccharide-Lyases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D012965:Sodium Chloride; D013045:Species Specificity; D013379:Substrate Specificity; D014733:Vibrio / Q000145:classification / Q000201:enzymology*
D000464:Alginates; D006603:Hexuronic Acids; D012965:Sodium Chloride; D020723:Glucuronic Acid; D011133:Polysaccharide-Lyases; C016158:poly(beta-D-mannuronate) lyase; D002122:Calcium Chloride