Reaction Specificity of Phospholipase D Prepared from Acinetobacter radioresistens a2 in Transphosphatidylation
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Updated: Feb 7, 2026
Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Kewei Cao1, Yanjun Liu1, Yingying Tian1,2
1College of Food Science and Engineering, Ocean University of China, 5 Yushan Road, 266003, Qingdao, Shandong Province, China.
Abstract:
Phospholipase D (PLD) can react with phospholipids as substrates, generally phosphatidylcholine (PtdCho), and the PLD-substrate intermediate can be cleaved by another alcohol, resulting in transphosphatidylation of the substrate, which can be used in the production of special lipids. In this study, the reaction conditions affecting the transphosphatidylation of PtdCho with serine were optimized and the reaction specificity of a novel PLD prepared from Acinetobacter radioresistens a2 was evaluated for transphosphatidylation with a variety of phospholipid substrates and head group donors. Based on the yield of phosphatidylserine, experimental kinetic data, maximum transphosphatidylation rate, and kinetic constant, the specificity of PLD in transphosphatidylation was found to be affected by unsaturated fatty-acid phospholipid substrates. The catalytic efficiency of PLD prepared from A. radioresistens a2 on the synthesis of natural phospholipids is on the order of l-serine > ethanolamine and glycerol ≫ inositol. Moreover, it was found that the transphosphatidylation of PtdCho with saccharides was related to the length of the carbon chain and the number of saccharide units.
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