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Synthesis and secretion of bacterial α‐amylase by the yeast Saccharomyces cerevisiae
Author(s) -
Kovaleva I.E.,
Novikova L.A.,
Luzikov Y.N.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81451-6
Subject(s) - periplasmic space , saccharomyces cerevisiae , yeast , cytoplasm , bacillus amyloliquefaciens , secretion , biochemistry , amylase , signal peptide , secretory pathway , secretory protein , saccharomyces , cell wall , intracellular , biology , alpha amylase , cell , chemistry , microbiology and biotechnology , enzyme , escherichia coli , recombinant dna , fermentation , gene , golgi apparatus
α‐Amylase from Bacillus amyloliquefaciens , synthesized in yeast Saccharomyces cerevisiae without substitution of the signal sequence, is efficiently secreted from yeast cells: 60–70% of the overall amount of the enzyme is found in the culture fluid. In contrast to many yeast secretory proteins, which accumulate in the periplasmic space and in the cell wall, intracellular α‐amylase is localized mainly in the cytoplasm. Obviously, transfer across the cell wall is not a rate‐limiting step in α‐amylase export from the cell. The glycosylated forms of proteins are predominantly found both inside the cell and in the culture medium.