Purification and characterization of an endo-polygalacturonase from a mutant of Saccharomyces 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.
Hirose
N
N
Department of Applied Biochemistry, Faculty of Agriculture, Osaka Prefecture University, Japan.
Kishida
M
M
Kawasaki
H
H
Sakai
T
T
D000911:Antibodies, Monoclonal / Q000737:chemistry; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007716:Kluyveromyces / Q000201:enzymology; D008970:Molecular Weight; D009154:Mutation; D011096:Polygalacturonase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D013696:Temperature
D000911:Antibodies, Monoclonal; D003470:Culture Media; D011096:Polygalacturonase