Mine_2003_Biotechnol.Lett_25_1863

Reference

Title : Stereochemistry of a diastereoisomeric amphiphile and the species of the lipase influence enzyme activity in the transesterification catalyzed by a lipase-co-lyophilizate with the amphiphile in organic media - Mine_2003_Biotechnol.Lett_25_1863
Author(s) : Mine Y , Fukunaga K , Yoshimoto M , Nakao K , Sugimura Y
Ref : Biotechnol Lett , 25 :1863 , 2003
Abstract :

Modified Candida rugosa and Pseudomonas cepacia lipase (CRL and PCL) were co-lyophilized with two pairs of synthetic diastereoisomeric amphiphiles, D- and L-2-(3-[bis-[3-(2,3,4,5,6-pentahydroxy-hexanoylamino)-propyl]-carbamoyl]-propiony lamino)-pentanedioic acid didodecyl ester (D- and L-BIG2C12CA); D- and L-2-(2,3,4,5,6-pentahydroxy-hexanoylamino)-pentanedioic acid didodecyl ester (D- and L-2C12GE). Enzyme activities of the modified lipase in the transesterification in organic solvent were evaluated. Both pairs of the diastereoisomeric amphiphiles showed enhanced enzyme activity in the transacetylation between racemic sulcatol and isopropenyl acetate in diisopropyl ether, catalyzed by the PCL-co-lyophilizate, by 19-48 fold when compared to the native lipase lyophilized from buffer alone independent of the stereochemistry of the amphiphiles, while in the case of the CRL-co-lyophilizate only the L-BIG2C12CA showed enhanced enzyme activity in the transbutyrylation between racemic solketal and vinyl butyrate in cyclohexane as high as 68-78 fold.

PubMedSearch : Mine_2003_Biotechnol.Lett_25_1863
PubMedID: 14677713

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Citations formats

Mine Y, Fukunaga K, Yoshimoto M, Nakao K, Sugimura Y (2003)
Stereochemistry of a diastereoisomeric amphiphile and the species of the lipase influence enzyme activity in the transesterification catalyzed by a lipase-co-lyophilizate with the amphiphile in organic media
Biotechnol Lett 25 :1863

Mine Y, Fukunaga K, Yoshimoto M, Nakao K, Sugimura Y (2003)
Biotechnol Lett 25 :1863