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• W1978208075 endingPage "1964" @default.
• W1978208075 startingPage "1959" @default.
• W1978208075 abstract "A new lipase (OBase) which efficiently hydrolyzes oleyl 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 gel-filtration HPLC under native conditions; these findings indicate that OBase is a monomeric enzyme. The optimum temperature and pH of OBase were about 45 degrees C and pH 8. Temperature and pH stabilities were at or lower than 35 degrees C 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." @default.
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• W1978208075 date "1999-01-01" @default.
• W1978208075 modified "2023-10-03" @default.
• W1978208075 title "Purification and Characterization of a Novel Extracellular Lipase Catalyzing Hydrolysis of Oleyl Benzoate from<i>Acinetobacter</i>nov. sp. Strain KM109" @default.
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• W1978208075 doi "https://doi.org/10.1271/bbb.63.1959" @default.
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