Purification and properties of collagenase from Cytophaga sp. L43-1 strain.
A collagenolytic bacterial strain was isolated from soil and was identified as Cytophaga sp. It produced several kinds of collagenase and protease. From the supernatant of a culture, a collagenase was purified as a single protein band upon SDS-PAGE and its molecular mass was estimated to be 120 kDa. Collagen and gelatin were good substrates for this enzyme. beta-Casein was cleaved by this enzyme at several sites.
Sasagawa
Y
Y
Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.
Kamio
Y
Y
Matsubara
Y
Y
Matsubara
Y
Y
Suzuki
K
K
Kojima
H
H
Izaki
K
K
D000595:Amino Acid Sequence; D002364:Caseins / Q000378:metabolism; D003094:Collagen / Q000378:metabolism; D017364:Collagenases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D003589:Cytophaga / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism; D005780:Gelatin / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000378:metabolism; D012988:Soil Microbiology; D013379:Substrate Specificity; D013696:Temperature
D002364:Caseins; D009842:Oligopeptides; D005780:Gelatin; D003094:Collagen; D010450:Endopeptidases; D017364:Collagenases