Purification and Characterization of an Endo-Polygalacturonase from a Mutant ofSaccharomyces cerevisiae | Zendy

Naoto Hirose | Zendy; Masao Kishida | Zendy; Haruhiko KAWASAKI | Zendy; Takuo Sakai | Zendy

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Purification and Characterization of an Endo-Polygalacturonase from a Mutant ofSaccharomyces cerevisiae

Author(s) -

Naoto Hirose,

Masao Kishida,

Haruhiko KAWASAKI,

Takuo Sakai

Publication year - 1999

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.63.1100

Subject(s) - kluyveromyces marxianus , pectinase , enzyme , biochemistry , saccharomyces cerevisiae , chemistry , mutant , molecular mass , enzyme assay , yeast , gene

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.

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