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• W1979968188 abstract "The presence of esterolytic activities in the intracellular extract of Lactococcus lactis subsp. lactis NCDO 763 was investigated. One major activity hydrolyzing β-naphthyl butyrate was detected. This activity was purified to homogeneity. The enzyme was a homotrimer; the molecular mass of the monomer was estimated by SDS-PAGE to be 29kDa; by mass spectrometry, it was 29655 ± 30 Da. The pI of the molecule was 4.5. The enzyme was active on para-nitrophenyl esters from C2 to C12 and on ortho-nitrophenyl butyrate, with a maximum activity on p-nitrophenyl butyrate. The optimum activity on this substrate was found at pH 8.0 and at 55 °C; kinetic parameters for this substrate were measured at 55 °C and were KM = 0.11 mM and Vmax = 8.17 μmol min−1. The enzyme was strongly inhibited by Pefabloc, diisopropyl fluoro-phosphate and 3,4-dichloroisocoumarin, demonstrating that it was a serine esterase. The amino-terminus of the enzyme was sequenced. The role of this enzyme in cheese ripening is discussed." @default.
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• W1979968188 date "1997-02-01" @default.
• W1979968188 modified "2023-09-24" @default.
• W1979968188 title "Intracellular esterase from Lactococcus lactis subsp. lactis NCDO 763: Purification and characterization" @default.
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• W1979968188 doi "https://doi.org/10.1016/s0958-6946(97)00001-0" @default.
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