Pectinolytic enzymes from Pseudomonas marginalis MAFF 03-01173.
Two pectinolytic enzymes were purified from the culture broth of Pseudomonas marginalis pv. marginalis MAFF 03-01173 with total 33% recovery of the initial activity. From the substrate specificities against pectin and polygalacturonic acid, the requirement of calcium ion for the enzymatic activity, and the N-terminal sequences, the enzymes were identified as pectin lyase and pectate lyase. The M,s of pectin lyase and pectate lyase were estimated to be 34,000 and 43,000, respectively, by SDS polyacrylamide gel electrophoresis. Both enzymes showed almost the same pH dependent activity curves with the highest activity at pH 8.3
Hayashi
K
K
Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology, Japan.
Inoue
Y
Y
Shiga
M
M
Sato
S
S
Takano
R
R
Hirayae
K
K
Hibi
T
T
Hara
S
S
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D010368:Pectins / Q000378:metabolism; D011133:Polysaccharide-Lyases / Q000302:isolation & purification* / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology*; D012967:Sodium Dodecyl Sulfate
D001426:Bacterial Proteins; D012967:Sodium Dodecyl Sulfate; D010368:Pectins; D011133:Polysaccharide-Lyases; C027349:pectin lyase; C023911:pectate lyase; C003181:polygalacturonic acid