A novel low molecular weight phospholipase D from Streptomyces sp. CS684.

Abstract With the aim of isolating economically viable enzymes from a microbial source, a novel phospholipase D (PLD) was purified from Streptomyces sp. CS684 (PLD 684 ). PLD 684 had molecular weight of 29 kDa, which makes it the second smallest PLD reported so far. The enzyme activity was optimum at pH 6 and 45 °C, and enhanced by various detergents. It was stable from pH 7 to 9 and at or below 45 °C when assayed after 40 h and 2 h, respectively. The K m and V max values for phosphatidylcholine were 1.16 mM and 1453.74 μmol min −1  mg −1 , respectively. It catalyzed the transphosphatidylation of glycerol, but not that of l -serine, myo -inositol or ethanolamine. Low molecular weight PLD 684 with transphosphatidylation activity may be utilized in the industrial production of rare and commercially important phospholipids.