Purification of the extracellular pectinolytic enzyme from the fungus Rhizopus oryzae NBRC 4707.
The pectinolytic enzyme from the solid-state culture of Rhizopus oryzae NBRC 4707 was purified to homogeneity by column chromatography on CM-Toyopearl 650 M and hydroxylapatite. The molecular weight of the enzyme was estimated by SDS-polyacrylamide gel electrophoresis to be 31,000 and was reduced to 29,700 after treatment with endoglycosidase H. Maximal activity was observed near pH 4.5 at 45 degrees C. The enzyme was shown to be endopolygalacturonase, as judged from the formation of oligogalacturonides as its reaction products. The addition of purified enzyme, as expected, enhanced the formation of lactic acid and ethanol in potato pulp grown with R. oryzae.
Saito
Katsuichi
K
National Agricultural Research Center for Hokkaido Region, Department of Upland Agriculture, Memuro, Hokkaido 082-0071, Japan.
Takakuwa
Naoya
N
Oda
Yuji
Y
D002852:Chromatography, Ion Exchange; D017886:Durapatite; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D000431:Ethanol / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007218:Industrial Microbiology; D019344:Lactic Acid / Q000096:biosynthesis; D008970:Molecular Weight; D011096:Polygalacturonase / Q000302:isolation & purification* / Q000378:metabolism*; D012233:Rhizopus / Q000201:enzymology*; D011198:Solanum tuberosum / Q000378:metabolism; D013696:Temperature
D019344:Lactic Acid; D000431:Ethanol; D017886:Durapatite; D006026:Glycoside Hydrolases; D011096:Polygalacturonase