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• W2022140101 endingPage "870" @default.
• W2022140101 startingPage "865" @default.
• W2022140101 abstract "Evidence was obtained that esterases purified from Streptococcus thermophilus ST1 and Lactococcus lactis subsp. cremoris B1079 are able to catalyse the synthesis of an ester (ethyl butanoate) in an aqueous environment via a transferase reaction (alcoholysis) in which fatty acyl (butyryl) groups from the glyceride (tributyrin) are transferred to the alcohol (ethanol). The esterases displayed transferase activity in which the acyl acceptor may be either water (hydrolysis) or alcohol (alcoholysis). The same enzymes were responsible for both activities. We propose that the esterases of St. thermophilus ST1 and Lc. lactis subsp. cremoris B1079 are alcohol acyltransferases that catalyse both hydrolysis and alcoholysis in an aqueous environment. This is the first report demonstrating ester synthesis by the esterases of these two lactic acid bacteria (LAB) via alcoholysis in an aqueous environment. Alcoholysis is the major mechanism of ester synthesis by the esterases of these two LAB in an aqueous environment." @default.
• W2022140101 created "2016-06-24" @default.
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• W2022140101 date "2004-10-01" @default.
• W2022140101 modified "2023-09-25" @default.
• W2022140101 title "Characterisation of esterases of Streptococcus thermophilus ST1 and Lactococcus lactis subsp. cremoris B1079 as alcohol acyltransferases" @default.
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• W2022140101 doi "https://doi.org/10.1016/j.idairyj.2004.02.014" @default.
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