Purification and some properties of six chitinases from Aeromonas sp. no. 10S-24.
Six chitinases were purified from a culture supernatant of Aeromonas sp. no. 10S-24 by ammonium sulfate precipitation, DEAE-Sephadex A-50, Butyl-Toyopearl 650M, and chromatofocusing. These enzymes were most active at pH 3.5-4.5 and the optimum temperature were 50 degrees C. The molecular weights of the enzymes were 89,000 to 120,000 from SDS-polyacrylamide gel electrophoresis. N-Terminal amino acid sequences of the enzymes were similar to that of chitinase I.
Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture, Japan.
M
M
Ueda
A
A
Fujiwara
T
T
Kawaguchi
M
M
Arai
D000333:Aeromonas / Q000201:enzymology*; D000595:Amino Acid Sequence; D002688:Chitinases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013696:Temperature
D007527:Isoenzymes; D002688:Chitinases