KAGAKU KOGAKU RONBUNSHU
Online ISSN : 1349-9203
Print ISSN : 0386-216X
ISSN-L : 0386-216X
Construction of an Esterase Model in Micellar Systems
Ryuichi UeokaYoko MatsumotoYasuo Kato
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JOURNAL FREE ACCESS

1991 Volume 17 Issue 3 Pages 518-523

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Abstract

The enantioselective hydrolysis of long-chain substrates (p-nitrophenyl N-dodecanoyl-D (L) -phenylalaninate : C12-D (L) -Phe-PNP) and p-nitrophenyl N-dodecanoyl-D (L) -leucinate : C12-D (L) -Leu-PNP) were carried out in cationic micellar (hexadecyltrimethylammonium chloride : CTAC ; hexadecylbenzyldimethylammonium chloride : CBzAC) systems. The rate constants for the hydrolysis of C12-L-Phe-PNP are markedly enhanced by N- (benzyloxycarbonyl) -L-phenylalanyl-L-histidine (Z-L-Phe L-His) through the efficient hydrophobic interaction between the L-Phe residues (in the Z-L-Phe-L-His catalyst and the L-form substrate). The enantioselectivity decreased from a value of kLa, obsd/kDa, obsd = 18 for the N- (benzyloxycarbonyl) -L-phenylalanyl-L-histidyl-L-leucine (Z-L-Phe-L-His-L-Leu) catalyst to that of kLa, obsd/kDa, obsd= 5.8 for the N-dodecanoyl-L-phenylalanyl-L-histidyl-L-leucine (C 12-L-Phe-L-His-L-Leu) catalyst having a long acyl chain. High enantioselectivity (kLa, obsd/kDa, obsd = 38) was attained for the hydrolysis of C12-D (L) -Phe-PNP as catalyzed by Z-L-Phe-L-His-L-Leu with CBzAC micelles above the critical micelle concentration through the efficient hydrophobic (recognizant) interaction between active tripeptide (Z-L-Phe-L-His-L-Leu), L-substrate (C12-L-Phe-PNP), and surfactant (CBzAC).

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© by THE SOCIETY OF CHEMICAL ENGINEERS, JAPAN
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