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Enzymes with lipase/acyltransferase activity for processing fats


Key words Enzyme, acyl transfer reaction, transesterification, biocatalysis, fat, oil, aqueous medium, process intensification, lipase, acyltransferase, triglyceride
Latest version 2012/10/05
Completed by INRA - IATE

How does it work?

Primary objective acyl transfer reactions in high yields, even in aqueous medium using enzymatic catalysis
Working principle The enzymes of interest combine the properties of lipases with the properties of acyltransferases: they can catalyze acyl tranfer reactions in a reaction mixture corresponding to a water activity greater than 0.8. (1, 2)

Both the expression system of the protein (vector, host cell, culture conditions, etc.) and the reaction conditions have been optimized (3). Consequently, the acyl transfer is possible in high yields (conversion yield up to 95%) (1)

Possible final products:

- alkyl esters : "biodiesel" (methyl or ethyl esters), isopropyl esters, etc.

- structured lipids : triglycerides enriched with polyunsaturated fatty acids (e.g. by interesterification of fish oils and vegetable oils) (2)

- emulsifiers : mono- and diacylglycerols, sucroesters, polyols esters etc.

- acylated peptides : currently they are obtained by chemical synthesis. They can have antioxidant or biological activity (4, 6); and food applications (5) : « By modifying food proteins with acylation, it is possible to increase the nutritional value of the protein, judging from growth tests on rats »

- acylated polyphenols (6): « flavonoids (aglycon, glycosylated) are widely used in pharmaceutic, cosmetic and food préparation. They have several physico-chemical properties and biological activities but they are characterized by a low solubility and stability. (…), the enzymatic acylation of these molecules with fatty and aromatic acids by protease and lipase (…) has been suggested as a promising route by several authors. (…). In fact, the position of acylation (regioselectivity) can drastically modify these properties. (…) »

Additional effects This technology allows much lower energy consumption than traditional acyl tranfer reactions with no use of organic solvents, using for example alcohols directly from fermentation broths
Important process parameters Reaction conditions (amounts of reactants and catalyst, temperature, duration, secondary reactions management, etc.), pH, enzyme activity, ionic strength
Important product parameters Choice of every element of the expression system (vector, host cell, culture conditions, purification steps, etc.).

What can it be used for?

Products Initial substrates: Triglycerides derived from fats and oils
Operations Conversion, esterification, processing of fats.

Alcoholysis of esters, alcoholysis of thio esters, thiolysis of esters, aminolysis of an ester with hydroxylamines or hydrazines, reaction of an ester with hydrogen peroxides and enantioselective synthesis of esters, thioesters, and lactones by alcoholysis. (4)

Solutions for short comings Improving/changing fats or oils properties

What can it NOT be used for?

Products Non triglycerides products
Operations Any other than transesterification
Other limitations This enzymatic catalysis does not work with free fatty acids; the substrates must be compatible with both the enzyme specificity for substrate and its optimal reaction conditions (temperature, pH, etc.)
Risks or hazards No information currently available


Maturity currently laboratory pilot scale
Modularity /Implementation This reaction works with standards reactors (packed-bed or CSTR) and sedimentation tank for phase separation
Consumer aspects Consumers may be reluctant to use products derived from GMOs.
Legal aspects Patent: WO03006644


Environmental aspects Low water and energy inputs, low toxicity of reactants and solvents

Further Information

Institutes INRA - IATE, INSA - LISBP
Companies Cognis
References (1) E. Dubreucq, F. Bigey, G. Moulin and A. Weiss, 2004. Enzymes with lipase/acyltransferase activity. EP1275711, WO03006644, CA 2 403 025 A1, CN12 15/54

(2) N. Osório, I. Maeiro, D. Luna and S. Ferreira-Dias, 2009. Interesterification of fat blends rich in Omega-3 polyunsaturated fatty acids catalyzed by immobilized lipase on modified sepiolite. New Biotechnology, Volume 25, Supplement 1, September 2009, Pages S111-S112.

(3) D. Dunweber, I.H. Jensen, L.B. Hansen, 2007. Method for producing acylated peptides. United States of America Patent 7273921, C07K1/00; C07K1/107; C07K14/575; C07K14/605; C07K14/62; C07K16/00; G01N33/00; G01N33/68; C07K1/00; C07K14/435; C07K16/00; G01N33/00; G01N33/68

(4) Hayasaka Tomoyuki and Uehara Keiichi, 2005. Characteristic and application of a novel acyl peptide. Fragr J, iss 0288-9803, vol 33, n°6, pages 81-87

(5) A. Ferjancic-Biagini, T. Giardina and A. Puigserver, 1998. Acylation of food proteins and hydrolysis by digestive enzymes : a review. Journal of Food Biochemistry, 22: 331–345

(6) L. Chebil, C. Humeau, A. Falcimaigne, J.M. Engasser, and M. Ghoul, 2006. Enzymatic acylation of flavonoids. Process Biochemistry Volume 41, Issue 11, November 2006, Pages 2237-2251

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Created by Hte inra on 21 June 2011, at 10:19