Fatty hydroxamic acid biosynthesis in aqueous medium in the presence of the lipase-acyltransferase from Candida parapsilosis.
The lipase-acyltransferase from Candida parapsilosis has been shown to catalyze fatty hydroxamic acid biosynthesis in a biphasic lipid/aqueous medium. The substrates of the reaction were an acyl donor (fatty acid or fatty acid methyl ester) and hydroxylamine. The transfer of acyl groups from a donor ester to hydroxylamine (aminolysis) was catalyzed preferentially to the reaction of free fatty acids. The highest synthesis activity was obtained in the presence of 1 M hydroxylamine at 45 degrees C and pH 6. This work confirmed the originality of the enzyme from Candida parapsilosis, which acts more like an acyltransferase than an hydrolase. This feature makes it an enzyme of choice for the direct bioconversion of oils in aqueous medium.
Vaysse
L
L
ENSA-INRA, UFR de Microbiologie Industrielle et de Génétique des Microorganismes, Montpellier, France.
Dubreucq
E
E
Pirat
J L
JL
Galzy
P
P
D000217:Acyltransferases / Q000737:chemistry / Q000378:metabolism*; D002175:Candida / Q000201:enzymology*; D006877:Hydroxamic Acids / Q000138:chemical synthesis* / Q000378:metabolism*; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D014867:Water
D006877:Hydroxamic Acids; D014867:Water; D000217:Acyltransferases; D008049:Lipase