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CONVERSION OF α‐KETO‐ISOCAPROIC ACID TO ISO‐AMYL ALCOHOL BY YEAST PYRUVATE DECARBOXYLASE AND ALCOHOL DEHYDROGENASE
Author(s) -
Watson T. G.,
Hough J. S.
Publication year - 1969
Publication title -
journal of the institute of brewing
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.523
H-Index - 51
eISSN - 2050-0416
pISSN - 0046-9750
DOI - 10.1002/j.2050-0416.1969.tb03226.x
Subject(s) - chemostat , isoamyl alcohol , pyruvate decarboxylase , chemistry , yeast , alcohol dehydrogenase , alcohol , biochemistry , pyruvate dehydrogenase kinase , isobutanol , pyruvate dehydrogenase complex , leucine , enzyme , biology , amino acid , bacteria , genetics
Brewer's yeast growing at a fixed rate in a chemostat in nitrogen‐limiting medium with leucine as nitrogen source produces about 100 times as much isoamyl alcohol as a culture with (NH 4 ) 2 SO 4 as nitrogen source. The maximum rate of decarboxylase activity towards α keto‐isocaproate is, however, the same for the two cultures, for a given maximum rate towards pyruvate. The control of isovaleraldehyde production is solely through the supply of α keto‐isocaproate. While alcohol dehydrogenase and nucleotide levels are the same for the two cell‐free extracts, those of the leucine‐grown cells show 2–3 times as great alcohol dehydrogenase activity towards isovaleraldehyde as those from cells grown on (NH 4 ) 2 SO 4 .