Purification and properties of lipase from the anaerobepropionibacterium acidi-propionici

Abstract

A lipase secreted by the anaerobePropionibacterium acidipropionici was purified 52-fold with 27% recovery by employing a three-step purification protocol. The enzyme has a small molecular mass (Mr = 6000–8000) as determined by gel filtration and ultracentrifugation. It hydrolyzed palm oil, coconut oil, castor oil, olive oil, groundnut oil and tributyrin. Enzyme activity was inhibited by Ni²⁺, Ba²⁺, Mg²⁺, Cu²⁺, ethylenediaminetetraacetic acid, iodoacetamide, N-acetylimidazole and nonidet P-40 but stimulated by Ca²⁺, Co²⁺, K⁺, Fe²⁺, sodium dodecyl sulfate and N-bromosuccinamide. The enzyme showed substrate inhibition for both tributyrin andp-nitrophenyl acetate.