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Use of Enzymes Deactivated by Site‐Directed Mutagenesis for the Preparation of Enantioselective Membranes
Author(s) -
Skolaut Alexander,
Rétey János
Publication year - 2002
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20020816)41:16<2960::aid-anie2960>3.0.co;2-i
Subject(s) - enantioselective synthesis , membrane , histidine , enantiomer , phenylalanine , chemistry , kinetic resolution , enzyme , phenylalanine ammonia lyase , mutagenesis , stereochemistry , lyase , site directed mutagenesis , biochemistry , catalysis , amino acid , mutation , mutant , gene
The conversion of enzymes into enantioselective receptors by mutagenesis opens the way for resolution of racemates by using enantioselective membranes: the transport of one enantiomer is accelerated through the membrane, while the other enantiomer diffuses across much more slowly. As an example, histidine ammonia lyase and phenylalanine ammonia lyase were rendered catalytically inactive and incorporated in artificial membranes (see figure). The facilitated transport of L ‐histidine and L ‐phenylalanine resulted in a maximum 14‐fold enantiomeric enrichment.