Extraction, purification and characterization of ADH1 from the budding yeast Kluyveromyces marxianus.
The enzyme ADH1 has been extracted and purified from the budding yeast Kluyveromyces marxianus, and its enzymatic activity has been compared, with the ADH1 extracted and purified in the same way from the well known yeast Saccharomyces cerevisiae. K. marxianus ADH1 has an optimal temperature higher than the S. cerevisiae enzyme (45-50 degrees vs 35 degrees C), a better stability to pH variations in the oxidative reaction (pH optimum 7.5), a lower Michaelis constant for acetaldehyde, and a good catalytic activity both for fermentative and oxidative reactions. In fact, while in Saccharomyces the constants ratio (velocity constant fermentation/velocity constant oxidation) is about 20,000, in Kluyveromyces the same ratio is only 15. Even if these two Genera are quite related (they belong to the same subfamily) it seems that their ADH1s possess different catalytic properties.
Pessione
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E
Dipartimento di Biologia Animale, Università, Torino.
Pergola
L
L
Cavaletto
M
M
Giunta
C
C
Trotta
A
A
Vanni
A
A
D000426:Alcohol Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism; D005285:Fermentation; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007716:Kluyveromyces / Q000201:enzymology*; D010084:Oxidation-Reduction; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D004718:Saccharomycetales / Q000201:enzymology*; D013696:Temperature
D000426:Alcohol Dehydrogenase