Isolation and characterization of chitinase from a flake-chitin degrading marine bacterium, Aeromonas hydrophila H-2330.
A flake-chitin degrading marine bacterium was isolated and identified as Aeromonas hydrophila. This strain secreted five chitinases and an beta-N-acetylglucosaminidase. The main chitinase (Chi-A) was purified and characterized. The optimum pH of Chi-A was 5-8, and the activity was inhibited by Hg2+ and Fe3+. Chi-A was different from chitinases of other Aeromonas species with respect to molecular weight (62,000) and insensitivity to monoiodoacetate. The amino-terminal amino acid sequence showed extensive similarity with chitinases from Gram-negative bacteria.
Hiraga
K
K
Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology, Japan.
Shou
L
L
Kitazawa
M
M
Takahashi
S
S
Shimada
M
M
Sato
R
R
Oda
K
K
D016980:Aeromonas hydrophila / Q000737:chemistry / Q000145:classification / Q000201:enzymology*; D000595:Amino Acid Sequence; D002686:Chitin / Q000378:metabolism; D002688:Chitinases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D002686:Chitin; D002688:Chitinases