Open AccessNADH reoxidation does not control glycolytic flux during exposure of respiring Saccharomyces cerevisiae cultures to glucose excess
Author(s) -
Brambilla L,
Bolzani D,
Compagno C,
Carrera V,
Dijken J.P,
Pronk J.T,
Ranzi B.M,
Alberghina L,
Porro D
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13423.x
Subject(s) - chemostat , biochemistry , fermentation , saccharomyces cerevisiae , glycolysis , lactate dehydrogenase , lactobacillus casei , biology , flux (metallurgy) , metabolism , chemistry , yeast , enzyme , bacteria , genetics , organic chemistry
of the Lactobacillus casei lactate dehydrogenase (LDH) gene into Saccharomyces cerevisiae under the control of the TPI1 promoter yielded high LDH levels in batch and chemostat cultures. LDH expression did not affect the dilution rate above which respiro‐fermentative metabolism occurred ( D c ) in aerobic, glucose‐limited chemostats. Above D c , the LDH‐expressing strain produced both ethanol and lactate, but its overall fermentation rate was the same as in wild‐type cultures. Exposure of respiring, LDH‐expressing cultures to glucose excess triggered simultaneous ethanol and lactate production. However, the specific glucose consumption rate was not affected, indicating that NADH reoxidation does not control glycolytic flux under these conditions.