title: A novel phospholipase D constitutively secreted by Ochrobactrum sp. ASAG-PL1 capable of enzymatic synthesis of phosphatidylserine.
abstract: Phospholipase D (PLD) plays a crucial role in the enzyme-mediated preparation of phosphatidylserine (PS). A new PLD constitutively secreted by Ochrobactrum sp. ASAG-PL1 is now reported for the first time. After purification, the MW of the enzyme was ~37 kDa by SDS-PAGE. Its activity was highest at 40 °C and pH 7.0 and more than 90 % of the initial activity was maintained after 30 days at 4 °C and pH 7.0. This enzyme may then be useful as a potential biocatalyst for PS production.
authors.affiliation: Hefei University of Technology, Hefei, 230009, People's Republic of China. fly5304471@gmail.com
authors.forename: Fei
authors.initials: F
authors.lastname: Hu
authors.forename: Huai
authors.initials: H
authors.lastname: Wang
authors.forename: Zhang-Qun
authors.initials: ZQ
authors.lastname: Duan
authors.forename: Ri-Sheng
authors.initials: RS
authors.lastname: Yao
mesh_terms: D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D042041:Ochrobactrum / Q000201:enzymology*; D010718:Phosphatidylserines / Q000096:biosynthesis*; D010739:Phospholipase D / Q000737:chemistry / Q000378:metabolism*; D013696:Temperature
chemical_list: D010718:Phosphatidylserines; D010739:Phospholipase D