Total seed oil and fatty acid methyl ester contents of Cuphea accessions

Phippen, Winthrop B.; Isbell, Terry A.; Phippen, Mary E.

doi:10.1016/j.indcrop.2006.02.001

Cited by 42 publications

(24 citation statements)

References 6 publications

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“…predominantly C12 and C14 and a small amount (0.2-1%) of C6 fatty acids [36-38]) and seeds of C. viscosissima (i.e. predominantly C8 and C10 fatty acids [39]). Therefore, acyl-ACP TEs in the seeds of these species are predicted to be specific for medium-chain acyl-ACPs.…”

Section: Resultsmentioning

confidence: 99%

Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity

et al. 2011

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BackgroundAcyl-acyl carrier protein thioesterases (acyl-ACP TEs) catalyze the hydrolysis of the thioester bond that links the acyl chain to the sulfhydryl group of the phosphopantetheine prosthetic group of ACP. This reaction terminates acyl chain elongation of fatty acid biosynthesis, and in plant seeds it is the biochemical determinant of the fatty acid compositions of storage lipids.ResultsTo explore acyl-ACP TE diversity and to identify novel acyl ACP-TEs, 31 acyl-ACP TEs from wide-ranging phylogenetic sources were characterized to ascertain their in vivo activities and substrate specificities. These acyl-ACP TEs were chosen by two different approaches: 1) 24 TEs were selected from public databases on the basis of phylogenetic analysis and fatty acid profile knowledge of their source organisms; and 2) seven TEs were molecularly cloned from oil palm (Elaeis guineensis), coconut (Cocos nucifera) and Cuphea viscosissima, organisms that produce medium-chain and short-chain fatty acids in their seeds. The in vivo substrate specificities of the acyl-ACP TEs were determined in E. coli. Based on their specificities, these enzymes were clustered into three classes: 1) Class I acyl-ACP TEs act primarily on 14- and 16-carbon acyl-ACP substrates; 2) Class II acyl-ACP TEs have broad substrate specificities, with major activities toward 8- and 14-carbon acyl-ACP substrates; and 3) Class III acyl-ACP TEs act predominantly on 8-carbon acyl-ACPs. Several novel acyl-ACP TEs act on short-chain and unsaturated acyl-ACP or 3-ketoacyl-ACP substrates, indicating the diversity of enzymatic specificity in this enzyme family.ConclusionThese acyl-ACP TEs can potentially be used to diversify the fatty acid biosynthesis pathway to produce novel fatty acids.

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Section: Resultsmentioning

confidence: 99%

Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity

et al. 2011

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“…The flow rate of carrier gas (nitrogen) was 1.0 mL min −1 . The oven temperature was kept at 60°C for 1 min and then rised at a speed of 40°C per minute to 240°C and kept at 240°C for 15 min . Injection volume of 1 μL was used for all samples.…”

Section: Methodsmentioning

confidence: 99%

Biocatalytic synthesis of vitamin A palmitate using immobilized lipase produced by recombinant Pichia pastoris

Yao

Lin

Yue

et al. 2017

Engineering in Life Sciences

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In this work, the Candida antarctica lipase B (CALB), produced by recombinant Pichia pastoris, was immobilized and used to synthesize vitamin A palmitate by transesterification of vitamin A acetate and palmitic acid in organic solvent. The reaction conditions including the type of solvent, temperature, rotation speed, particle size, and molar ratio between the two substrates were investigated. It turned out that the macroporous resin HPD826 serving as a carrier showed the highest activity (ca. 9200 U g −1 ) among all the screened carriers. It was found that the transesterification kinetic of the immobilized CALB followed the ping pong Bi-Bi mechanism and the reaction product acetic acid inhibited the enzymatic reaction with an inhibition factor of 2.823 mmol L −1 . The conversion ability of the immobilized CALB was 54.3% after 15 cycles. In conclusion, the present work provides a green route for vitamin A palmitate production using immobilized CALB to catalyze the transesterification of vitamin A acetate and palmitic acid.

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“…L'acide gras en formation est allongé, par ajouts successifs de 2 Carbones, grâce à des molécules de malonyl-CoA (Jane, 2005). Grâce à son indice de saponification élevé et à sa forte proportion en acides gras saturés, l'huile de coco peut être utilisée dans la fabrication de savon et de détergent (Phippen et al, 2006).…”

Section: Teneurs En Acides Gras Des Huilesunclassified

Caractérisation physico-chimiques des noix et de l’huile des premiers cocotiers (<i>Cocos nucifera</i> L.) PB 121 issus de la culture <i>in vitro</i> d’embryon zygotique plantés en Côte d’Ivoire

Deffan¹,

Konan²,

Assa³

et al. 2013

Int. J. Bio. Chem. Sci

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Le présent travail vise à évaluer les caractéristiques physico-chimiques de noix et de l'huile d'amande des premiers cocotiers PB 121 issus de la culture in vitro. Les observations ont été faites sur des noix de trois stades de maturité puis comparées avec celles des cocotiers PB 121 plantés ordinairement (PB 121 O). Il en ressort que les masses des noix PB 121 O sont significativement supérieures à celles issues de culture in vitro (PB 121 V), pendant que celles d'amande sont moins élevées. Les teneurs en huiles augmentent généralement au cours de la maturation jusqu'au rang 25 à 70,80% chez PB 121 O et 69,78% chez PB 121 V. Elles baissent ensuite respectivement jusqu'à 65,44% et 64,78%. Les indices d'acide et d'iode sont moins élevés chez les PB 121 V avec respectivement au rang 24 sont de 5,33 et 33,00% puis 5,89 et 39,98% chez PB 121 O. Les indices de saponification de PB 121 V sont supérieurs à ceux de PB 121 O. L'acide laurique représente l'acide gras le plus abondant des huiles étudiées. L'huile d'amande de PB 121 V qui est plus stable et moins acide est plus appropriée en savonnerie.

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Total seed oil and fatty acid methyl ester contents of Cuphea accessions

Cited by 42 publications

References 6 publications

Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity

Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity

Biocatalytic synthesis of vitamin A palmitate using immobilized lipase produced by recombinant Pichia pastoris

Caractérisation physico-chimiques des noix et de l’huile des premiers cocotiers (<i>Cocos nucifera</i> L.) PB 121 issus de la culture <i>in vitro</i> d’embryon zygotique plantés en Côte d’Ivoire

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