Lipase-catalyzed reactions in organic media: competition and applications

Deleuze, Hervé; Langrand, G.; Millet, Horace; Baratti, J.; Buono, Gérard; Triantaphylidès, C.

doi:10.1016/0167-4838(87)90278-0

Cited by 74 publications

(34 citation statements)

References 16 publications

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“…cExpressed as pm01 mint (unit of hydrolytic activity >-I. dRelative standard deviation 5 10%. Table I shows that in toluene, K, values for n-octanol, chosen because it is a good nucleophile for this lipase (Rangheard et al, 1992) increased similarly for both enzyme forms with increasing a, This result can be explained on the basis that water competes with the alcohol for the acyl enzyme intermediate to give butyric acid, whose presence in the reaction medium was evidenced by G L C. The competition between water and alcohols for the acyl enzyme intermediate has been clearly demonstrated and quantified in the case of lipases in organic media by Deleuze et al (1987). For instance, with Candida cylindracea lipase the competitive factor of water for the butyryl enzyme had a value intermediate between that of cyclohexanol and that of isopentanol.…”

Section: Resultsanddiscussionmentioning

confidence: 88%

Effects of water activity on Vmax and KM of lipase catalyzed transesterification in organic media

Bovara¹,

Carrea²,

Ottolina³

et al. 1993

Biotechnol Lett

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The V,, and KM of various forms of lipase from Pseudomonas cepacia ( powder, adsorbed onto Celite or covalently linked to polyethylene glycol ) were determined in organic solvents preequilibrated to water activities ( a, ) from ~0.1 to 0.84. The model reaction was the transesterification between n-octanol and vinyl butyrate. It was found that Ki,., for the nucleophile increased with increasing a, for all three lipase forms. V,, increased with increasing a, for polyethylene glycol-lipase, whereas there was an optimum at intermediate a, values ( 0.11 -0.38 ) for lipase powder and Celite-immobilized lipase.

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Section: Resultsanddiscussionmentioning

confidence: 88%

Effects of water activity on Vmax and KM of lipase catalyzed transesterification in organic media

Bovara¹,

Carrea²,

Ottolina³

et al. 1993

Biotechnol Lett

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“…The competitive factor (also commonly referred to as relative selectivity constant or α-value) among multiple FA substrates was determined based on the kinetic model advanced previously (6,18) as applied in previous studies (8)(9)(10). α-Values were analyzed experimentally as progress of reactivity of one (or more) substrate(s) relative to a reference substrate (C8 FA in this study), according to the following equation: [1] where subscripts A and B represent competing substrates and the reference substrate, respectively.…”

Section: Methodsmentioning

confidence: 99%

Reaction selectivity of Burkholderia cepacia (PS‐30) lipase as influenced by monoacylation of sn‐glycerol

Parkin

2004

J Americ Oil Chem Soc

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Reaction selectivities were determined in multicompetitive reactions mediated by Burkholderia cepacia lipase (Amano PS-30) at a water activity of 0.19 in hexane. Saturated FA (C4-C18 even chain) and oleic acid (C18:1) were reacted with a single alcohol, glycerol, or α-or β-MAG, containing C4, C10, C16, or C18:1 individually as alcohol cosubstrate. Similar ordinal patterns of FA selectivity, with C8, C10, and C16 preferred over others, were generally observed for incorporation of FA into specific acylglycerol (AG) pools of the 24 specific cases evaluated. The three exceptions were enrichment of C14 and C18 in the MAG pool with α-C16-MAG substrate, and a general suppression of >C8 incorporation into the TAG pool for reactions with α-C10-and α-C16-MAG. PS-30 lipase selectivity toward MAG was in descending order: α/β-C4-MAG > β-C10-MAG > β-C16-MAG > α/β-C18:1-MAG > α-C10-MAG > α-C16-MAG. Selectivity in channeling CX of the original CX-MAG substrates into higher AG species was in descending order: α-Generally, MAG were better acyl donors than FA for esterification reactions leading to DAG formation. These observations are relevant to the design of biocatalytic processes intended to yield specifically structured TAG.A focus of over a decade of recent research on exploiting the synthetic power of lipases in organic media is the prospect of preparing value-added or functional "structured glycerides" for food and pharmaceutical industries (1). Examples of lipids modified by lipase to confer additional value and/or functionality include low-calorie fats (2), cocoa butter substitutes (3), and nutritional lipids (4,5). The applications-driven research in this area has focused largely on using specific lipid mixtures or even pure reaction components to prepare specific targets of synthesis. Much of this body of literature has been rather empirical and sparingly reliant on features of lipase selectivity, such as regioselectivity. Indeed, the commercial and economic justifications for using a lipase over any chemical modification process are embedded in the multifaceted patterns of selectivity offered by an enzymatic reaction.To facilitate the broadest possible application of lipases to modify lipids for added value, it is imperative to develop an understanding of lipase selectivity patterns in a manner that allows the application of such knowledge to a host of possible reactions, where the identity and levels of lipid substrates may be quite varied. One approach that fulfills this need is the determination of relative kinetic constants that define the substrate selectivity patterns of various lipases. Selectivity constants may be used to predict the pattern of lipase reactivity under a broad range of conditions where substrate identity and levels are variable, since kinetic constants are not concentration-dependent. Many groups have used this approach to quantify the discriminatory power of various lipases among substrates for esterification reactions between FA and alcohols (6-10).Our approach has focused on kinetically chara...

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“…It has been shown for C. cylindracea lipase that a carboxylic acid in organic media is a better acyl donor than its alkyl ester (Deleuze et al 1987). The 2-methyldecanoic acid produced during hydrolysis will, due to its amphiphilic character, accumulate in the interface between the ester substrate and the water.…”

Section: -Methyldecanoic Acidmentioning

confidence: 99%

Reaction conditions for the resolution of 2-methylalkanoic acids in esterification and hydrolysis with lipase from Candida cylindracea

Holmberg¹,

Holmquist²,

Hedenström³

et al. 1991

Appl Microbiol Biotechnol

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We have demonstrated resolution of 2-methylalkanoic acids using lipase from Candida cylindracea as a catalyst. The resolution of 2-methyldecanoic acid was more successful than that of 2-methylbutyric acid both by esterification and hydrolysis. This indicates that the resolution of the acid is dependent on the chain length of the acid moiety. The chain length of the alcohol moiety of the ester affected the resolution of the long-chain acid only. Using esterification, (R)-2-methyldecanoic acid was produced in an enantiomeric excess (e.e.) of 95% (E = 40). If the enantiomeric ratio is low (E--3.6), as in the resolution of 2-methylbutyric acid, esterification combined with a high equilibrium conversion could be used to yield the remaining acid in a high e.e. In the hydrolytic reactions, the e.e. and the equilibrium conversion were dependent on the pH and the presence of CaCI2. When octyl 2-methyldecanoate was hydrolysed at pH 8.0 in the presence of CaC12, the (S)-aeid was formed with an e.e. of 80% (E= 9), but when the hydrolysis was carried out at pH 7.5 without CaCI2, a very low e.e. and a low equilibrium conversion were observed. The latter conditions allowed the esterification of 2-methyldecanoic acid with 1-octanol even in aqueous medium.

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Lipase-catalyzed reactions in organic media: competition and applications

Cited by 74 publications

References 16 publications

Effects of water activity on Vmax and KM of lipase catalyzed transesterification in organic media

Effects of water activity on Vmax and KM of lipase catalyzed transesterification in organic media

Reaction selectivity of Burkholderia cepacia (PS‐30) lipase as influenced by monoacylation of sn‐glycerol

Reaction conditions for the resolution of 2-methylalkanoic acids in esterification and hydrolysis with lipase from Candida cylindracea

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