STEREOSELECTIVE HYDROLYSIS OF AMINO-ACID ESTERS BY DIPEPTIDE CATALYSTS AND BY N-DECANOYL-HISTIDINE IN SURFACTANT AGGREGATE DOMAINS

被引:1
|
作者
IHARA, Y [1 ]
NAKANISHI, E [1 ]
AKIYAMA, A [1 ]
YAMAMOTO, H [1 ]
机构
[1] UNIV OSAKA PREFECTURE,DEPT APPL CHEM,SAKAI,OSAKA 591,JAPAN
关键词
Amino Acids--Performance - Catalysts--Biological Materials - Chemical Reactions--Catalysts - Enzymes--Performance - Surface Active Agents--Applications;
D O I
10.1002/pola.1989.080270108
中图分类号
O63 [高分子化学(高聚物)];
学科分类号
070305 ; 080501 ; 081704 ;
摘要
The rate constants of hydrolysis of the enantiomers of amino acid nitrophenyl esters by catalytic domains composed of cationic surfactant aggregates and either dipeptide catalysts or Ni-decanoyl-L-histidine have been determined at pH 7.30. The dipeptide catalysts show large range enhancement and stereoselectivity in aggregate domains. The surfactant structural effects are examined by investigation of the rate constants and stereoselectivities, and the nature of stereoselective catalysis is discussed.
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页码:87 / 97
页数:11
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