Characterisation of esterases of Streptococcus thermophilus ST1 and Lactococcus lactis subsp. cremoris B1079 as alcohol acyltransferases

Autor:	M.D. Bennett, Vaughan L. Crow, K Baker, Ross Holland, Shao-Quan Liu, Gillian E. Norris
Rok vydání:	2004
Předmět:	Streptococcus thermophilus Ethanol biology Tributyrin Lactococcus lactis subsp cremoris Lactococcus lactis biology.organism_classification Applied Microbiology and Biotechnology Lactic acid chemistry.chemical_compound Hydrolysis chemistry Biochemistry Acyltransferases bacteria Food Science
Zdroj:	International Dairy Journal. 14:865-870
ISSN:	0958-6946
DOI:	10.1016/j.idairyj.2004.02.014
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::f5d334eac0bbbbe04498b747877a26c6 https://doi.org/10.1016/j.idairyj.2004.02.014 Zobrazit plný text záznamu Full Text from ScienceDirect