Bioreduction of ketones mediated by baker's yeast with acetate as ultimate reducing agent.
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چکیده
منابع مشابه
Sucrose Inversion by Bakers' Yeast as a Function of Temperature
Inversion of sucrose by bakers' yeast follows the same course as inversion catalyzed by yeast invertase. Rate of inversion increases exponentially with temperature; the temperature characteristic in the Arrhenius equation is 10,700 below 13-17 degrees C., and 8,300 above that temperature. Temperature inactivation occurs above 40 degrees C. The effects of temperature upon rate of inversion were ...
متن کاملSucrose Inversion by Bakers' Yeast as a Function
where k is the rate of the reaction, z is a constant, e is 2.718, R is the gas constant, T is the absolute temperature, and # represents the energy of activation in calories per tool of the pacemaker reaction in the catenary series of events controlling the rate (Crozier and Hoagland, 1934). Since most biological reactions are catalyzed by enzymes, the change in rate is determined by the enzyme...
متن کاملTHE CALCIUM BINDING SITES OF THE BAKERS' YEAST TRANSKETOLASE
The calcium binding sites of Bakers' Yeast Transketolase (TK) was elucidated by estimating the pKa values of the functional groups that bind to calcium. These pKa's were found to be 6.25 and 7.2 relating to the pKa's of the two immidazol moieties of histidine residues on the enzyme. The rate of the binding of calcium to the enzyme was obtained separately as a function of pH. Maximum values ...
متن کاملDNA polymerases from bakers' yeast.
Two DNA polymerases are present in extracts of commercial bakers' yeast and wild type Saccharomyces cerevisiae grown aerobically to late log phase. Yeast DNA polymerase I and yeast DNA polymerase II can be separated by DEAE-cellulose, hydroxylapatite, and denatured DNA-cellulose chromatography from the postmitochondrial supernatants of yeast lysates. The yeast polymerases are both of high molec...
متن کاملFormaldehyde dehydrogenase from bakers' yeast.
In the course of studies of formaldehyde metabolism in yeast (I), an enzyme was found that catalyzed the oxidation of formaldehyde in the presence of glutathione and diphosphopyridine nucleotide. A similar enzyme was discovered independently by Strittmatter and Ball in liver (2). This paper describes the partial purification and some of the properties of yeast formaldehyde dehydrogenase. Some e...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1991
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.55.867