ミセル系エステラーゼモデルの構築

DOI Web Site Web Site

書誌事項

タイトル別名
  • Construction of an Esterase Model in Micellar Systems.
  • ミセルケイ エステラーゼ モデル ノ コウチク
公開日
1991
DOI
  • 10.1252/kakoronbunshu.17.518
公開者
公益社団法人 化学工学会

この論文をさがす

説明

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).

収録刊行物

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ