Z. Olama et al., PURIFICATION AND CHARACTERIZATION OF GLYCEROL PHOSPHATE DEHYDROGENASEPRODUCED FROM WHEAT BRAN USING A MIXED CULTURE SYSTEM, Food chemistry, 51(1), 1994, pp. 33-37
Glycerol phosphate dehydrogenase was produced from wheat bran by the m
ixed culture fermentation technique. The process involved saccharifica
tion of cellulose to glucose by Trichoderma viride followed by convers
ion of glucose into glycerol by Saccharomyces cerevisiae Y-1347. Diffe
rent purification steps were applied to the culture filtrate to obtain
a pure enzyme preparation. The pure preparation indicated that the mo
lecule consists of one peptide chain, with a molecular weight of 51 00
0 and isoelectric point of 5.7. The amino acid content was also studie
d. Lineweaver-Burk analysis gave a k(m) value of 0.033 mmol and V-max
of 83.3 mmol/ml/min. The enzyme showed its maximum activity at pH 6.0
when incubated at 25 degrees C for 10 min.