화학공학소재연구정보센터
Bioresource Technology, Vol.100, No.3, 1388-1393, 2009
A novel low molecular weight phospholipase D from Streptomyces sp CS684
With the aim of isolating economically viable enzymes from a microbial source, a novel phospholipase D (PLD) was purified from Streptomyces sp. CS(684) (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 degrees C, and enhanced by various detergents. It was stable from pH 7 to 9 and at or below 45 degrees 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 mu mol 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. (c) 2008 Elsevier Ltd. All rights reserved.