Peculiar properties of lipase fromCandida parapsilosis (Ashford) langeron and talice

Abstract

A new Candida parapsilosis lipase was isolated and studied. This enzyme was purified by hydrophobic chromatography on a phenyl-sepharose CIAB column followed by gel permeation on a Sephacryl $300 HR column. It was a 160 kg'mo1-1 molecular-weight oligomeric enzyme. Optimal activity was obtained at 45°C and pH 6.5. The lipase activity toward various acylglycerols and esters was studied. The hydrolysis rate was greater for secondary acylesters than for primary acylesters. This lipase showed a high specificity for long-chain fatty acids and particularly for polyunsaturated fatty acids. This enzyme was able to catalyze the synthesis of various oleoylesters in aqueous medium.

The 3D model of the lipase/acyltransferase from Candida parapsilosis, a tool for the elucidation of structural determinants in CAL-A lipase superfamily

“…Within the few lipases able to catalyze alcoholysis preferentially to hydrolysis in aqueous media, the lipase/acyltransferase CpLIP2 from C. parapsilosis appears as the best candidate today for the development of lipid bioconversions and functionalizations without a strict control of a w [14,19,23] and has been described as of high industrial interest [41][42][43][44]. With CpLIP2, competition of a short chain alcohol with water has been shown to be highly favorable to the alcohol, even with a high a w and a low thermodynamic activity of the alcohol [9,14,18,21,23]. Transesterification with this enzyme appears thus kinetically controlled (very low rate of hydrolysis versus high rate of alcoholysis), which allows the production of new esters at concentrations above the thermodynamic equilibrium of hydrolysis/esterification.…”

“…Such enzymes and their applications have been described for several years by our group. The first one was the CpLIP2 lipase/acyltransferase from Candida parapsilosis [17][18][19][20][21], followed by CaLIP4 from Candida albicans [22] and CtroL4 from Candida tropicalis [23]. These lipases/acyltransferases have been shown to be homologous to C. albicans lipase 1 and CAL-A, the lipase A of P. antarctica (formerly designated as Candida antarctica) [20,24] and to belong to the P. antarctica lipase A-like α/β hydrolase superfamily (abH38) [23,25,26] of the Lipase Engineering Database [27].…”

Enzymatic fatty esters synthesis in aqueous medium with lipase from Candida parapsilosis (Ashford) Langeron and Talice

“…Furthermore, it is known that the polyunsaturated fatty acids in natural oils are generally located on a glycerol internal position. 3) Riaublanc (1993) studied the hydrolysis activity of Candida parapsilosis in various homogeneous acylglycerols and esters. He demonstrated that the specificity of hydrolysis activity increased with the degree of fatty acid unsaturation.…”

“…This was not observed during the transfer reactions catalysed by the free lipase from Candida cylindracea, when the transesterification kinetics increased with the substrate or enzyme hydration until saturation of the phases (Goldberg CT al., 1990). This paper describes alcoholysis of rapeseed oil by methanol, catalysed by the lipase from ('nndida parnpsilosis described by Riaublanc (1993) in a biphasic liquid/liquid medium consisting of a lipid emulsion in an aqueous medium containing free enzyme and alcohol in solution.…”

Staphylococcal lipases stereoselectively hydrolyse the sn-2 position of monomolecular films of diglyceride analogs. Application to sn-2 hydrolysis of triolein

“…It can therefore tentatively be concluded that CALA and all the staphylococcal lipases tested hydrolyse triolein in the sn-2 position. In a previous study, Riaublanc et al [51] reported that a lipase from Candida parapsilosis (Ashford) hydrolysed secondary acylesters faster than primary acylesters. When rapeseed oil was used as the substrate, similar amounts of 1,2(2,3) and 1,3 diacylacylglycerol were measured by these authors.…”