Purification and Properties of Lysophospholipase Produced by Corticium centrifugum

Lysophospholipase (EC 3. 1. 1. 5) from the culture broth of Corticium centrifugum was purified 92-fold in specific activity by DEAE-Sephadex and hydroxylapatite column chromatography. The isoelectric point was at about pH 3.9, and the molecular weight was about 130,000. The optimal pH was about 3.5~5.0. The stable pH range was from 7.0 to 8.0. Lysophospholipase activity was inhibited by Fe³⁺, Hg²⁺ and Al³⁺, but stimulated by various organic solvents. Diazobenzene p-sulfonic acid, N-bromosuccinimide and diisopropyl-fluorophosphate also inhibited the activity. This enzyme did not hydrolyze mono-, di-or tripalmitin or phosphatidylcholine. Apparent Michaelis constants of lysophospholipase activity for 1-acyl-LPC, 1-palmitoyl-LPC and 1-oleoyl-LPC were 0.35, 0.16 and 0.09 mm, respectively. The effect of detergents on the enzyme activity was observed to differ with the fatty acid composition of substrate.