Biotechnology and the fats and oils industry — An overview

Rattray, J. B. M.

doi:10.1007/bf02582132

Cited by 52 publications

(20 citation statements)

References 130 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One factor is the inheri of the enzyme. The other factor is the availabilit CoA, which is influenced by its concentration (whel has been reached), the temperature, and the occurr competing acyl CoAs There is an increasing interest in using both classical breeding enhancement and modern biotechnology to improve the quality of seed oils ubility of the (5,12,15 …”

Section: Discussionmentioning

confidence: 99%

“…The two enzymes were more active on oleoyl CoA than on erucoyl CoA at high acyl CoA concentrations (10 and 20 micromolar) at 24°C, but were more active on erucoyl CoA than on oleoyl CoA at low acyl CoA concentrations (1.36 micromolar or less) at 32 and 40°C. These findings are discussed in terms of the contribution of the enzyme to the acyl specificity in storage triacylglycerols and the implication in seed oil biotechnology.it is assumed that the in vivo pool sizes ofthe acyl CoAs determine the acyl specificity in the 3-position of the triacylglycerol.In seed oil biotechnology, one major goal is to alter the chain length of the fatty acyl moiety of the triacylglycerols (5,12,15 In an attempt to resolve part of the above unknown, we have studied the acyl CoA preference of seed diacylglycerol acyltransferase. We also would like to see if the enzyme exerts preference on specific acyl CoA, such that this preference reflects the acyl moiety in the triacylglycerol.…”

mentioning

confidence: 99%

“…In seed oil biotechnology, one major goal is to alter the chain length of the fatty acyl moiety of the triacylglycerols (5,12,15 In an attempt to resolve part of the above unknown, we have studied the acyl CoA preference of seed diacylglycerol acyltransferase. We also would like to see if the enzyme exerts preference on specific acyl CoA, such that this preference reflects the acyl moiety in the triacylglycerol.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Acyl Coenzyme A Preference of Diacylglycerol Acyltransferase from the Maturing Seeds of Cuphea, Maize, Rapeseed, and Canola

Cao¹,

Huang²

1987

Plant Physiol.

View full text Add to dashboard Cite

ABSTRACrIn their seed triacylglycerols, Cuphea carthagenensis contains 62% lauric acid; maize possesses 50% linoleic acid and 30% oleic acid; rapeseed (Brassica napus L. var Dwarf Essex) has 40% erucic acid; and Canola (Brassica napus L. var Tower) holds 60% oleic acid and 23% linoleic acid. Diacylglycerol acyltransferase (EC 2.3.1.20) in the microsomal preparations fron maturing seeds of the above species were tested for their preference in using different forms of acyl coenzyme A (CoA). Lauroyl CoA, oleoyl CoA, and erucoyl CoA individually or in equimolar mixtures at increasing concentrations were added to the assay mixture containing diolein, and the formation of trinacylglycerols from the acyl groups at 24, 32, and 40°C was analyzed. The Cuphea enzyme preferred lauroyl CoA to oleoyl CoA, and was inactive on erucoyl CoA. The maize enzyme had about equal activities on oleoyl CoA and lauroyl CoA, and was inactive on erucoyl CoA. Enzymes from both rapeseed and Canola had the same pattern of acyl CoA preference, with highest activities on lauroyl CoA. The two enzymes were more active on oleoyl CoA than on erucoyl CoA at high acyl CoA concentrations (10 and 20 micromolar) at 24°C, but were more active on erucoyl CoA than on oleoyl CoA at low acyl CoA concentrations (1.36 micromolar or less) at 32 and 40°C. These findings are discussed in terms of the contribution of the enzyme to the acyl specificity in storage triacylglycerols and the implication in seed oil biotechnology.it is assumed that the in vivo pool sizes ofthe acyl CoAs determine the acyl specificity in the 3-position of the triacylglycerol.In seed oil biotechnology, one major goal is to alter the chain length of the fatty acyl moiety of the triacylglycerols (5,12,15 In an attempt to resolve part of the above unknown, we have studied the acyl CoA preference of seed diacylglycerol acyltransferase. We also would like to see if the enzyme exerts preference on specific acyl CoA, such that this preference reflects the acyl moiety in the triacylglycerol. The enzyme was obtained from four selected oil seeds which have unique and very contrasting fatty acyl moieties in the triacylglycerols. MATERIALS AND METHODSIn oil seeds, the fatty acid composition of the storage triacylglycerols is species-and variety-specific, and environmental factors such as temperature exert some modifying effects (13, 16). Within a seed species, the fatty acid composition in each of the three positions of a triacylglycerol is also largely inherited (16).In oil seeds as well as in mammalian tissues, triacylglycerols are synthesized from acyl CoA and glycerol-P via three different acyltransferases (1,13,16,17). The first two acyltransferases (glycerol-P acyltransferase and lysophosphatidic acid acyltransferase) possess some acyl CoA preference, such that their specificities as well as the in vivo pool sizes of acyl CoAs produce the observed positional acyl specificity in the triacylglycerol (1,17

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Acyl Coenzyme A Preference of Diacylglycerol Acyltransferase from the Maturing Seeds of Cuphea, Maize, Rapeseed, and Canola

Cao¹,

Huang²

1987

Plant Physiol.

View full text Add to dashboard Cite

show abstract

“…(17). In this endeavor, the focus DISCUSSION has been on genetic engineering of the fatty acid synthetase complex which catalyses the elongation of fatty acid.…”

Section: Assay Of Lpa-at Activitymentioning

confidence: 99%

Lysophosphatidate Acyltransferase Activities in the Microsomes from Palm Endosperm, Maize Scutellum, and Rapeseed Cotyledon of Maturing Seeds

Huang²

1989

Plant Physiol.

View full text Add to dashboard Cite

Lysophosphatidate (LPA) acyltransferase (EC 2.3.1.51) in the microsomes from palm endosperm (Syagrus cocoides Martius), maize scutellum (Zea mays L.), and rapeseed cotyledon (Brassica napus L.) of maturing seeds were studied for their specificities toward the acyl moiety of the substrates lysophosphatidate and acyl coenzyme A (CoA). The LPA acceptor greatly influenced the acyl CoA specificity of the enzyme and vice versa. With 1-oleoyllysophosphatidate (LPA-18:1), the palm enzyme was equally active on oleoyl CoA and lauroyl CoA, whereas the maize and rapeseed enzymes were more active on oleoyl CoA than on lauroyl CoA. With 1-lauroyl-lysophosphatidate (LPA-12), which generated less activity than LPA-18:1, the palm enzyme was three times more active on lauroyl CoA than on oleoyl CoA. LPA-12 was an inactive substrate for the maize and rapeseed enzymes. The selectivity of the enzymes was also studied using a mixture of LPA-18:1 and LPA-12, as well as lauroyl CoA and oleoyl CoA. Under this selectivity condition and compared to the specificity condition, the enzymes from all the three seeds exerted stronger preference for oleoyl moiety in either the LPA or acyl CoA, and again, only the palm enzyme could act on LPA-12.Similar studies, although in lesser detail, showed that the enzymes from soybean and castor bean were similar to the maize and rapeseed enzymes in having little activity on substrates containing lauroyl moiety. The results demonstrate the importance of the acyl group in the sn-I position of LPA in determining the acyl preference in the sn-2 position in phosphatidate synthesis. The palm enzyme appears to be the only one capable of synthesizing phosphatidates containing high amounts of lauric moieties.In oil seeds, TAG3 synthesis proceeds via the Kennedy pathway (20). Glycerol-3-P is first acylated by glycerol-3-P AT at the sn-l position to form lysophosphatidate, which undergoes a second acylation by LPA-AT to form phosphatidate.

show abstract

“…They affect the composition of the lipid hydrolysis products (in hydrophilic reaction media) or the composition of new triglycerides and other molecules (in hydrophobic reaction media) (Macrae, 1983;Rattray, 1984 Most extracellular microbial lipases exhibit little fatty acid specificity when incubated with natural fats and oils (Macrae, 1983). The Geotrichum candidum lipase was found to possess a fatty acid specificity in the hydrolysis of esters of a particular type of long-chain fatty acid (Jensen, 1974).…”

Section: Introductionmentioning

confidence: 99%

Specificity of <i>Mucor miehei</i> lipase on methyl ester substrates

Aggelis¹,

Komaitis²,

Pina³

et al. 1993

Grasas y Aceites

View full text Add to dashboard Cite

RESUMEN Especificidad de lipasa Mucor miehei en sustrato de esteres metí-licos.Los esteres metílicos de ácidos grasos constituyen un buen sustrato para la caracterización de tipos de especificidad de iipasa. En el presente trabajo, se estudió la acción hidrolítica de lipasa de Mucor miehei. Se demostró que esta lipasa cataliza preferencialmente la hidrólisis de esteres metílicos de ácidos grasos con número pequeño de dobles enlaces. Se encontró también que esta lipasa muestra una especificidad en la hidrólisis de ásteres metílicos de ácidos grasos con cadena alifática corta. PALABRAS-CLAVE: Especificidad Ester metílico -Lipasa (Mucor SUMMARY Specificity of Mucor miehei lipase on methyl ester substrates.Fatty acid methyl esters constitute a good substrate for the characterization of lipase typospecificity. In the present work, the hydrolytic action of lipase from Mucor mietiei was studied. It was demonstrated that this lipase preferentially catalyses the hydrolysis of fatty acid methyl esters with small number of double bonds. It was also found that this lipase shows a specificity in the hydrolysis of fatty acid methyl esters with short aliphatic chain. KEY-WORDS: Lipase (Mucor mieliei) -Metliyl ester -Specificity -Substrate.

show abstract

Biotechnology and the fats and oils industry — An overview

Cited by 52 publications

References 130 publications

Acyl Coenzyme A Preference of Diacylglycerol Acyltransferase from the Maturing Seeds of Cuphea, Maize, Rapeseed, and Canola

Acyl Coenzyme A Preference of Diacylglycerol Acyltransferase from the Maturing Seeds of Cuphea, Maize, Rapeseed, and Canola

Lysophosphatidate Acyltransferase Activities in the Microsomes from Palm Endosperm, Maize Scutellum, and Rapeseed Cotyledon of Maturing Seeds

Specificity of <i>Mucor miehei</i> lipase on methyl ester substrates

Contact Info

Product

Resources

About