Purification and Characterization of an Endo-Polygalacturonase from a Mutant ofSaccharomyces cerevisiae
Copyright policy )Purification and Characterization of an Endo-Polygalacturonase from a Mutant ofSaccharomyces cerevisiae
An extracellular endo-polygalacturonase (PGase) produced by a mutant of Saccharomyces cerevisiae was isolated. The enzyme was regarded, immunologically, as a PGase belonging to the Kluyveromyces marxianus group. The enzyme had properties similar to the PGase from K. marxianus in heat and pH stability, and N-terminal amino acid sequence. However, the enzyme showed different properties in optimum pH and temperature, molecular weight, and reactivity in antiserum against PGase from K. marxianus, indicating that the enzyme has a different molecular structure from the PGase from K. marxianus.
- Osaka Metropolitan University Japan
- Kindai University Japan
Temperature, Antibodies, Monoclonal, polygalacturonase, Saccharomyces cerevisiae, Hydrogen-Ion Concentration, Culture Media, <i>Saccharomyces cerevisiae</i>, Molecular Weight, Kluyveromyces, Polygalacturonase, Mutation, Electrophoresis, Polyacrylamide Gel, mutant
Temperature, Antibodies, Monoclonal, polygalacturonase, Saccharomyces cerevisiae, Hydrogen-Ion Concentration, Culture Media, <i>Saccharomyces cerevisiae</i>, Molecular Weight, Kluyveromyces, Polygalacturonase, Mutation, Electrophoresis, Polyacrylamide Gel, mutant
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