Industrial use of lipases to produce fatty acid esters

Hills, G. Loftus

doi:10.1002/ejlt.200300853

Cited by 146 publications

(96 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Currently, the dominant natural source for high-quality WE is jojoba oil, though its high price limits most of its possible applications to cosmetic and medical products. WE may also be produced chemically or with immobilized lipases (39). Thus, there is at present and will be in the future a demand for an economically feasible biotechnological production of inexpensive jojoba oil-like WE from inexpensive substrates (40).…”

Section: Biotechnological Relevance Of Tag and Wementioning

confidence: 99%

Acyltransferases in Bacteria

Röttig

Steinbüchel

2013

Microbiol Mol Biol Rev

151

141

View full text Add to dashboard Cite

SUMMARY Long-chain-length hydrophobic acyl residues play a vital role in a multitude of essential biological structures and processes. They build the inner hydrophobic layers of biological membranes, are converted to intracellular storage compounds, and are used to modify protein properties or function as membrane anchors, to name only a few functions. Acyl thioesters are transferred by acyltransferases or transacylases to a variety of different substrates or are polymerized to lipophilic storage compounds. Lipases represent another important enzyme class dealing with fatty acyl chains; however, they cannot be regarded as acyltransferases in the strict sense. This review provides a detailed survey of the wide spectrum of bacterial acyltransferases and compares different enzyme families in regard to their catalytic mechanisms. On the basis of their studied or assumed mechanisms, most of the acyl-transferring enzymes can be divided into two groups. The majority of enzymes discussed in this review employ a conserved acyltransferase motif with an invariant histidine residue, followed by an acidic amino acid residue, and their catalytic mechanism is characterized by a noncovalent transition state. In contrast to that, lipases rely on completely different mechanism which employs a catalytic triad and functions via the formation of covalent intermediates. This is, for example, similar to the mechanism which has been suggested for polyester synthases. Consequently, although the presented enzyme types neither share homology nor have a common three-dimensional structure, and although they deal with greatly varying molecule structures, this variety is not reflected in their mechanisms, all of which rely on a catalytically active histidine residue.

show abstract

Section: Biotechnological Relevance Of Tag and Wementioning

confidence: 99%

Acyltransferases in Bacteria

Röttig

Steinbüchel

2013

Microbiol Mol Biol Rev

151

141

View full text Add to dashboard Cite

show abstract

“…These compounds have odors of different fruits and are parts of complex mixtures providing specific aromas. Longer chain acids esters (C 18 ) are used in cosmetic industry as emollient for personal care applications [1].…”

Section: Introductionmentioning

confidence: 99%

Synthesis of alkyl esters by cutinase in miniemulsion and organic solvent media

Barros

Fonseca

Cabral

et al. 2009

Biotechnology Journal

View full text Add to dashboard Cite

High conversion yields of 95 % at equilibrium after 8h of reaction in iso-octane for pentanoic acid (C 5 ) with ethanol at equimolar concentration (0.1M) was achieved.Additionally, this work also shows that a significant and unexpected change in cutinase selectivity occurred for longer chain length carboxylic acids (C 8 -C 10 ) in miniemulsion system comparing with organic solvent (iso-octane) and previous studies in reverse micellar systems where a selectivity towards short chain fatty acids ( C 4 -C 6 ) was observed. The possibility to work with higher concentration of substrates ,without inhibitiory effect on enzyme, was another advantage of miniemulsion system.

show abstract

“…However, the high price of jojoba oil has limited its use, which is currently restricted to medical and cosmetics applications as a basis for ointments, creams, and other care products. Today, wax esters are mainly produced chemically or by biotechnological processes employing immobilized lipases (10). However, even the lipase-based biotechnological wax ester production depends on fatty alcohols as substrates, which at present must be synthesized chemically.…”

mentioning

confidence: 99%

Neutral Lipid Biosynthesis in Engineered Escherichia coli : Jojoba Oil-Like Wax Esters and Fatty Acid Butyl Esters

Kalscheuer

Stöveken

Luftmann

et al. 2006

Appl Environ Microbiol

113

View full text Add to dashboard Cite

Wax esters are esters of long-chain fatty acids and long-chain fatty alcohols which are of considerable commercial importance and are produced on a scale of 3 million tons per year. The oil from the jojoba plant (Simmondsia chinensis) is the main biological source of wax esters. Although it has a multitude of potential applications, the use of jojoba oil is restricted, due to its high price. In this study, we describe the establishment of heterologous wax ester biosynthesis in a recombinant Escherichia coli strain by coexpression of a fatty alcohol-producing bifunctional acyl-coenzyme A reductase from the jojoba plant and a bacterial wax ester synthase from Acinetobacter baylyi strain ADP1, catalyzing the esterification of fatty alcohols and coenzyme A thioesters of fatty acids. In the presence of oleate, jojoba oil-like wax esters such as palmityl oleate, palmityl palmitoleate, and oleyl oleate were produced, amounting to up to ca. 1% of the cellular dry weight. In addition to wax esters, fatty acid butyl esters were unexpectedly observed in the presence of oleate. The latter could be attributed to solvent residues of 1-butanol present in the medium component, Bacto tryptone. Neutral lipids produced in recombinant E. coli were accumulated as intracytoplasmic inclusions, demonstrating that the formation and structural integrity of bacterial lipid bodies do not require specific structural proteins. This is the first report on substantial biosynthesis and accumulation of neutral lipids in E. coli, which might open new perspectives for the biotechnological production of cheap jojoba oil equivalents from inexpensive resources employing recombinant microorganisms.

show abstract

Industrial use of lipases to produce fatty acid esters

Cited by 146 publications

References 5 publications

Acyltransferases in Bacteria

Acyltransferases in Bacteria

Synthesis of alkyl esters by cutinase in miniemulsion and organic solvent media

Neutral Lipid Biosynthesis in Engineered Escherichia coli : Jojoba Oil-Like Wax Esters and Fatty Acid Butyl Esters

Contact Info

Product

Resources

About