Lipase-catalyzed transesterification in organic solvent: effects of water and solvent, thermal stability and some applications

Hirata, Hirofumi; Higuchi, Katsuhiko; Yamashina, Takao

doi:10.1016/0168-1656(90)90004-u

Cited by 66 publications

(28 citation statements)

References 18 publications

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“…The reaction was conducted at 37°C and 150 rpm. Substrate and product concentrations were determined by GC assay and optical purity was determined by chiral HPLC wicz and Keese 1989 ;Klibanov 1986;Dordick 1989;Khmelnitsky et al 1988;Engel et al 1991;Geresh and Gilboa 1991;Hirata et al 1990;Kirchner et al 1985;Macrae 1983; Y a m a d a and Shimizu 1988). Lipases are commercially used in interesterification reactions in the oil and fat industry to modify the composition and physical properties o f triglycerides (Matsuo et al 1981).…”

Section: Resultsmentioning

confidence: 99%

Enantioselective enzymatic acetylation of racemic [4-[4?,6? (E)]]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-hydroxy-2H-pyran-2-one

Patel

McNamee

Szarka

1992

Appl Microbiol Biotechnol

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A chiral compound [4R-[4c~,6fl(E)l]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-hydroxy-2H-pyran-2-one (R-(+)-1) was prepared by the lipase-catalysed stereoselective acetylation of racemic 1 in an organic solvent. Chiral R-(+)-I is a hydroxymethyl glutaryl coenzyme A (HMG CoA) reductase inhibitor and a potential anticholesterol drug candidate. Among various lipases evaluated, lipase PS-30 from P s e u d o m o n a s species efficiently catalysed acetylation of the undesired enantiomer of racemic 1 to yield the S-(-)-acetylated product 2 and unreacted desired R-( + )-1. A reaction yield of 48 mol%0 and an optical purity of 98% were obtained for R-( + )-1 when the reaction was conducted in toluene as solvent in the presence of isopropenyl acetate as acyl donor. Lipase PS-30 was immobilized on Accurel polypropylene (PP) and the immobilized enzyme was reused (five cycles) in the acetylation reaction without loss of enzyme activity, productivity, or optical purity of the R-(+ )-1. The enzymatic acetylation process was scaled-up to 501 and a 640-1 volume (preparative batches) at a substrate concentration of 4 g/1. R-(+)-I was recovered from the preparative batches in 68-71% recovery yield with 99.4% gas chromatography homogeneity index and 98.5% optical purity. The S-(-) acetate 2 produced by the acetylation reaction was enzymatically hydrolysed by lipase PS-30 in a biphasic system to prepare the corresponding S-( -)-1.

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Section: Resultsmentioning

confidence: 99%

Enantioselective enzymatic acetylation of racemic [4-[4?,6? (E)]]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-hydroxy-2H-pyran-2-one

Patel

McNamee

Szarka

1992

Appl Microbiol Biotechnol

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“…Enzymatic reactions in organic media at high temperatures have also been reported several times in the literatures. 15,22) Enzyme deactivation at high temperatures is caused by the formation of a scrambled structure, cleavage of disulfide bonds, deamidation of asparagine or glutamine, and hydrolysis of aspartic acid residues. These reactions all require water.…”

Section: Resultsmentioning

confidence: 99%

“…20 ,22,23) Hirata et al 22 ) reported that the optimal water content was related to the partition equilibrium of water between enzymes and solvents. They suggested that the hydration of enzyme with water was a significant factor in the expression of enzyme activity.…”

Section: Effects Of Water Content On Interesterijicationmentioning

confidence: 99%

Interesterification of Triglyceride and Fatty Acid in a Microaqueous Reaction System Using Lipase–Surfactant Complex

Isono¹,

Nabetani²,

Nakajima³

1995

Bioscience, Biotechnology, and Biochemistry

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“…The function of water in the enzymatic reactions in nonpolar solvents is not fully understood; however, it has been discussed in terms of hydration of enzyme (Klibanov, 1986;Yamane et al, 1988;Zaks and Klibanov, 1988;Han et al, 1990;Hirata et al, 1990). The R-activity profile for both enzymes exhibited a bell-shaped curve with maximum rate at R ϭ 18 for R. javanicus lipase and R ϭ 13 for C. rugosa lipase.…”

Section: Effect Of Reaction Parameters On Milk Fat Hydrolysismentioning

confidence: 99%

Hydrolysis of Milk Fat By Lipase in Solvent‐free Phospholipid Reverse Micellar Media

Patel

Nagarajan

Kilara

1996

Journal of Food Science

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Butterfat was hydrolyzed with lipases contained in lecithin reverse micelles. The influence of pH, temperature, molar ratio of surfactant to water (R) and surfactant concentration on the hydrolytic reaction indicated linear, quadratic, and interactive effects for reaction systems mediated by R. javanicus and C. rugosa lipases. The initial reaction rate was dependent on reaction parameters; however, the degree of hydrolysis was independent of pH. Both enzymes exhibited high thermal stability. The content and composition of milk fat hydrolysates prepared by R. javanicus lipase were most influenced by reaction temperature and R. The optimum conditions for production of free fatty acids, monoacylglycerols, diacylglycerols and specific regio-isomers were defined.

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Lipase-catalyzed transesterification in organic solvent: effects of water and solvent, thermal stability and some applications

Cited by 66 publications

References 18 publications

Enantioselective enzymatic acetylation of racemic [4-[4?,6? (E)]]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-hydroxy-2H-pyran-2-one

Enantioselective enzymatic acetylation of racemic [4-[4?,6? (E)]]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-hydroxy-2H-pyran-2-one

Interesterification of Triglyceride and Fatty Acid in a Microaqueous Reaction System Using Lipase–Surfactant Complex

Hydrolysis of Milk Fat By Lipase in Solvent‐free Phospholipid Reverse Micellar Media

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