Glyceride synthesis catalyzed by cutinase using the monomolecular film technique

Melo, Eduardo P.; Ivanova, М.; Aires-Barros, M. Raquel; Cabral, J. M. S.; Verger, R.

doi:10.1021/bi00005a018

Cited by 14 publications

(7 citation statements)

References 9 publications

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“…Lyophilized cutinase has also been used as a powder suspension to elucidate its mechanism of action, in stereoselectivity, specificity (Mannesse et al, 1995a,b;Rogalska et al, 1997;Zandonella et al, 1995), and kinetic (Sjursnes et al, 1998) studies, including esterification (Melo et al, 1995c;Sarazin et al, 1992Sarazin et al, , 1995 and transesterification (Lamare and Legoy, 1995;Lamare et al, 1997;Parvaresh et al, 1992) reactions. Cutinase was immobilized onto solid supports, either adsorbed or covalently coupled, and used in hydrolysis (Gonçalves et al, 1995(Gonçalves et al, , 1996a(Gonçalves et al, ,b, 1999Zoungrana, 1997), esterification (Sereti et al, 1997;Sjursnes et al, 1998), and transesterification (Fontes et al, 1998;Lamare and Legoy, 1995;Lamare et al, 1997;Parvaresh et al, 1992;Serralha et al, 1998) reactions.…”

Section: Preparation Of Cutinase For Use As a Biocatalystmentioning

confidence: 99%

“…The synthesis of oleoylglycerides, monoolein, diolein, and triolein, catalyzed by lyophilized cutinase, was demonstrated (Melo et al, 1995c) using the monomolecular film technique previously used to study the kinetics of lipase hydrolysis. The water subphase was replaced by glycerol, and a film of oleic acid was initially spread on the glycerol surface.…”

Section: Esterificationmentioning

confidence: 99%

See 1 more Smart Citation

Cutinase: From molecular level to bioprocess development

Carvalho¹,

Aires-Barros²,

Cabral³

1999

Biotechnol. Bioeng.

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216

138

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Section: Preparation Of Cutinase For Use As a Biocatalystmentioning

confidence: 99%

Section: Esterificationmentioning

confidence: 99%

Cutinase: From molecular level to bioprocess development

Carvalho¹,

Aires-Barros²,

Cabral³

1999

Biotechnol. Bioeng.

Self Cite

216

138

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“…Lyophilized cutinase has been used to elucidate its mechanism of reaction, in stereoselectivity, specificity (Rogalska et al, 1997;Mannesse et al, 1995a;Mannesse et al, 1995b;Zandonella et al, 1995) and kinetic (Sjursnes et al, 1998) studies, including esterification (Sarazin et al, 1992;Sarazin et al, 1995;Melo et al, 1995a) and transesterification (Parvaresh et al, 1992;Lamare and Legoy, 1995;Lamare et al, 1997) reactions. Lyophilized cutinase was also added to an aqueous/triolein biphasic system to perform the hydrolysis of this triglyceride into oleic acid and glycerol (Flipsen et al, 1996).…”

Section: A Preparation Of Cutinase To Be Used As a Biocatalyst In Nomentioning

confidence: 99%

“…Kinetic studies allowed the determination of the apparent kinetic parameters, K m (pentanol)=208 mM and K m (lauric acid)=60 mM. The synthesis of oleoyl glycerides, monoolein, diolein and triolein, catalyzed by lyophilized cutinase was demonstrated (Melo et al, 1995a) using the monomolecular film technique previously used to study the kinetics of lipase hydrolysis. The water subphase was replaced by glycerol, and a film of oleic acid was initially spread on the glycerol surface.…”

Section: Esterificationmentioning

confidence: 99%

Cutinase structure, function and biocatalytic applications

Carvalho¹,

Aires‐Barros²,

Cabral³

1998

Electron. J. Biotechnol.

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This review analyses the role of cutinases in nature and their potential biotechnological applications. The cloning and expression of a fungal cutinase from Fusarium solani f. pisi, in Escherichia coli and Saccharomyces cerevisiae hosts are described. The three dimensional structure of this cutinase is also analysed and its function as a lipase discussed and compared with other lipases. The biocatalytic applications of cutinase are described taking into account the preparation of different cutinase forms and the media where the different types of enzymatic reactions have been performed, namely hydrolysis, esterification, transesterification and resolution of racemic mixtures. The stability of cutinase preparations is discussed, particularly in anionic reversed micelles considering the role of hexanol as substrate, co-surfactant and stabilizer. Process development based on the operation of cutinase reactors is also reviewed.Cutinases are hydrolytic enzymes that degrade cutin, the cuticular polymer of higher plants, which is a polyester composed of hydroxy and epoxy fatty acids (Purdy and Kolattukudy, 1975). The fatty acids of cutin are usually n-C 16 and n-C 18 and contain one to three hydroxyl groups. Ester bonds predominate in the cutins, although peroxide bridges and ether linkages have also been presented.Cutin plays a key role in protection against the entry of pathogens into plants, and its enzymatic degradation has proved to be one of the first steps in the infection process.

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“…They can also be used for hydrolysis reactions in the dairy industry, in household detergents, and in the oleochemical industry (1). Furthermore, they can be used for the synthesis of mono-, di-, and triglycerides (8), and under low water activities, they are able to catalyze transesterification reactions (9)(10)(11)(12)(13). Additionally, they can selectively esterify fatty acids with different alcohols (12,14,15).…”

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confidence: 99%

Three New Cutinases from the Yeast Arxula adeninivorans That Are Suitable for Biotechnological Applications

Bischoff

Litwińska

Cordes³

et al. 2015

Appl Environ Microbiol

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The genes ACUT1, ACUT2, and ACUT3, encoding cutinases, were selected from the genomic DNA of Arxula adeninivorans LS3. The alignment of the amino acid sequences of these cutinases with those of other cutinases or cutinase-like enzymes from different fungi showed that they all had a catalytic S-D-H triad with a conserved G-Y-S-Q-G domain. All three genes were overexpressed in A. adeninivorans using the strong constitutive TEF1 promoter. Recombinant 6؋ His (6h)-tagged cutinase 1 protein (p) from A. adeninivorans LS3 (Acut1-6hp), Acut2-6hp, and Acut3-6hp were produced and purified by immobilized-metal ion affinity chromatography and biochemically characterized using p-nitrophenyl butyrate as the substrate for standard activity tests. All three enzymes from A. adeninivorans were active from pH 4.5 to 6.5 and from 20 to 30°C. They were shown to be unstable under optimal reaction conditions but could be stabilized using organic solvents, such as polyethylene glycol 200 (PEG 200), isopropanol, ethanol, or acetone. PEG 200 (50%, vol/vol) was found to be the best stabilizing agent for all of the cutinases, and acetone greatly increased the half-life and enzyme activity (up to 300% for Acut3-6hp). The substrate spectra for Acut1-6hp, Acut2-6hp, and Acut3-6hp were quite similar, with the highest activity being for short-chain fatty acid esters of p-nitrophenol and glycerol. Additionally, they were found to have polycaprolactone degradation activity and cutinolytic activity against cutin from apple peel. The activity was compared with that of the 6؋ His-tagged cutinase from Fusarium solani f. sp. pisi (FsCut-6hp), also expressed in A. adeninivorans, as a positive control. A fed-batch cultivation of the best Acut2-6hp-producing strain, A. adeninivorans G1212/YRC102-ACUT2-6H, was performed and showed that very high activities of 1,064 U ml ؊1 could be achieved even with a nonoptimized cultivation procedure.

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Glyceride synthesis catalyzed by cutinase using the monomolecular film technique

Cited by 14 publications

References 9 publications

Cutinase: From molecular level to bioprocess development

Cutinase: From molecular level to bioprocess development

Cutinase structure, function and biocatalytic applications

Three New Cutinases from the Yeast Arxula adeninivorans That Are Suitable for Biotechnological Applications

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