Purification of L-asparaginase from a bacteria Erwinia carotovora and effect of a dihydropyrimidine derivative on some of its kinetic parameters

391-394L-Asparaginase shows antileukemic activity and is generally administered in the body in combination with other anticancer drugs like pyrimidine derivatives. In the present study, L-asparaginase was purified from a bacteria Erwinia carotovora and the effect of a dihydropyrimidine derivative (1-amino-6-methyl-4-phenyl-2-thioxo, 1,2,3,4-tetrahydropyrimidine-5-carboxylic acid methyl ester) was studied on the kinetic parameters Km and Vmax of the enzyme using L-asparagine as substrate. The enzyme had optimum activity at pH 8.6 and temperature 35°C, both in the absence and presence of pyrimidine derivative and substrate saturation concentration at 6 mg/ml. For the enzymatic reaction in the absence and presence (1 to 3 mg/ml) of dihydropyrimidine derivative, Km values were 7.14, 5.26, 4.0, and 5.22 M, and Vmax values were 0.05, 0.035, 0.027 and 0.021 mg/ml/min, respectively. The kinetic values suggested that activity of enzyme was enhanced in the presence of dihydropyrimidine derivative

Enzymatic saccharification of cellulosic waste by cellulase system of <i style="">Cellulomonas uda</i> immobilized on tri(4-formyl phenoxy) cyanurate

816-819Cellulose is one of the most abundant non-degradable organic compound on earth. Near about half of the municipal and agricultural solid wastes contain cellulose or their derivatives. Saccharification or enzymatic hydrolysis of cellulosic wastes liberates glucose. In the present work, cellulase from Cellulomonas uda was extracted, partially purified by dialysis and immobilized on an organic support namely tri(4-formyl phenoxy) cyanurate. Percentage saccharification of seven different cellulosic waste materials was studied using native and immobilized cellulase systems. Maximum saccharification for both native and immobilized cellulase was observed for sawmill dust or wood dust (4.9 and 2.4% respectively) as compared to other cellulosic waste substrates