Acylphosphatase increases the rate of ethanol production from glucose in cell-free extracts of Saccharomyces cerevisiae.
Addition of acylphosphatase exerted a stimulating effect on the alcoholic fermentation of glucose by Saccharomyces cerevisiae. The rates of glucose degradation and ethanol production by cell-free extracts of the S-288C strain were measured in the absence and in the presence of various levels of this enzyme. Two acylphosphatase isoenzymes were used; one was purified from horse skeletal muscle and the other from human erythrocytes. Both increased the rate of alcoholic fermentation, but that from erythrocytes proved to be the more efficient. This stimulating action is probably due to an "uncoupling effect" of acylphosphatase on the fermentative process, through hydrolysis of 3-phosphoglyceroyl phosphate. This was demonstrated by the fact that alcoholic fermentation was stimulated considerably by a mixture of ADP and inorganic phosphate and by arsenate as well. The possibility of improving the fermentative capacity of microorganisms may have important biotechnological applications.
Ramponi
G
G
Dipartimento di Scienze Biochimiche, Universitá di Firenze, Florence, Italy.
Liguri
G
G
Nediani
C
C
Stefani
M
M
Taddei
N
N
Nassi
P
P
D017766:Acid Anhydride Hydrolases; D000431:Ethanol / Q000378:metabolism*; D005656:Fungal Proteins; D005947:Glucose / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis / Q000494:pharmacology*; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000378:metabolism*; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D000431:Ethanol; D005656:Fungal Proteins; D005947:Glucose; D010744:Phosphoric Monoester Hydrolases; D000097024:Acylphosphatase