Purification and Characterization of a Novel Extracellular Lipase Catalyzing Hydrolysis of Oleyl Benzoate from Acinetobacter nov. sp. Strain KM109

概要

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A new lipase (OBase) which efficiently hydrolyzesoleyl benzoate (OB) was found in the culture supernatant of Acinetobacter nov. sp. strain KM109,a new isolate growing in a minimum medium containing OB as the sole carbon source. OBase was purified to homogeneity with 213-fold purification and 0.8% yield. The molecular weight was estimated to be 62,000±1,000 by SDS-PAGE under denatured-reduced conditions and to be 50,000±1,000 by gelfiltration HPLC under native conditions ; these findings indicate that OBase is a monomeric enzyme. The optimum temperature and pH of OBase were about 45℃ and pH 8. Temperature and pH stabilities were at or lower than 35℃ and in a range of pH 6-8,respectively. Purified OBase preferentially hydrolyzed p-nitrophenyl benzoate (pNPB) over p-nitrophenyl acetate (pNPA) or p-nitrophenyl caproate (pNPC) [pNPB/pNPA = 20 and pNPB/pNPC = 5.4], indicating that OBase has a high affinity for benzoyl esters. Partial amino-acid sequences of OBase fragments obtained after lysyl endopeptidase treatment showed no similarity with known proteins.
社団法人日本農芸化学会の論文
1999-11-23