By Overexpression in the Yeast Pichia pastoris to Enhanced Enantioselectivity: New Aspects in the Application of Pig Liver Esterase.

Stable product quality without the interfering influences of other isoenzymes and hydrolases is possible through the application of recombinant pig liver esterase (rPLE), for which functional expression has now been achieved for the first time. In the hydrolysis of 1-phenyl-2-butyl acetate rPLE leads to substantially higher enantioselectivity than commercial PLE preparations.

[1]  W. Junge,et al.  Characterization of the isoenzymes of pig-liver esterase. 1. Chemical Studies. , 1979, European journal of biochemistry.

[2]  C. Sih,et al.  Quantitative analyses of biochemical kinetic resolutions of enantiomers , 1982 .

[3]  C. Schmidt-Dannert,et al.  Cloning, Functional Expression, and Characterization of Recombinant Pig Liver Esterase , 2001, Chembiochem : a European journal of chemical biology.

[4]  R. Verger,et al.  Lipases: Interfacial Enzymes with Attractive Applications. , 1998, Angewandte Chemie.

[5]  M. C. Tedford,et al.  Application of Pig Liver Esterases (PLE) in Asymetric Synthesis , 1990 .

[6]  U. Bornscheuer.  Directed Evolution of Enzymes for Biocatalytic Applications , 2001 .

[7]  F. Arnold.  Design by Directed Evolution , 1998 .

[8]  U. Bornscheuer,et al.  Hydrolases in Organic Synthesis: Regio- and Stereoselective Biotransformations , 1999 .

[9]  A. Puigserver,et al.  Purification and molecular cloning of porcine intestinal glycerol-ester hydrolase--evidence for its identity with carboxylesterase. , 1998, European journal of biochemistry.

[10]  E. Toone,et al.  Enzymes in organic synthesis. 42. Investigation of the effects of the isozymal composition of pig liver esterase on its stereoselectivity in preparative-scale ester hydrolysis of asymmetric synthetic value , 1988 .

[11]  M. Nishizawa,et al.  Stereoselective production of (+)-trans-chrysanthemic acid by a microbial esterase: cloning, nucleotide sequence, and overexpression of the esterase gene of Arthrobacter globiformis in Escherichia coli , 1995, Applied and environmental microbiology.

[12]  U. Bornscheuer.  Gerichtete Evolution von Enzymen , 1998 .

[13]  A. Ikai,et al.  Electron microscopic and biochemical evidence that proline‐β‐naphthylamidase is composed of three identical subunits , 1991, FEBS letters.

[14]  C. Schmidt-Dannert,et al.  High-Level Formation of Active Pseudomonas cepaciaLipase after Heterologous Expression of the Encoding Gene and Its Modified Chaperone in Escherichia coli and Rapid In Vitro Refolding , 1999, Applied and Environmental Microbiology.

[15]  R. Schmid,et al.  Lipasen: Grenzflächen‐Enzyme mit attraktiven Anwendungen , 1998 .

[16]  Kurt Faber,et al.  Biotransformations in Organic Chemistry , 1992 .

[17]  W. Junge,et al.  Characterization of the isoenzymes of pig-liver esterase. 2. Kinetic studies. , 1979, European journal of biochemistry.

[18]  W. Jencks,et al.  Different forms of pig liver esterase. , 1980, Archives of biochemistry and biophysics.

[19]  U. Bornscheuer,et al.  Screening, Nucleotide Sequence, and Biochemical Characterization of an Esterase from Pseudomonas fluorescens with High Activity towards Lactones , 1999, Applied and Environmental Microbiology.

[20]  A. Gutman,et al.  Convenient practical resolution of racemic alkyl-aryl alcohols via enzymatic acylation with succinic anhydride in organic solvents , 1993 .

[21]  U. Bornscheuer,et al.  Characterization and enantioselectivity of a recombinant esterase from Pseudomonas fluorescens , 1998 .

[22]  C. Schmidt-Dannert,et al.  Overexpression of lipase A and B of Geotrichum candidum in Pichia pastoris : High-level production and some properties of functional expressed lipase B , 1997 .

[23]  Kenji Takahashi,et al.  The nucleotide and deduced amino acid sequences of porcine liver proline‐β‐naphthylamidase , 1991 .

[24]  J. B. Jones.  Esterases in organic synthesis: present and future , 1990 .

[25]  K. Hult,et al.  Enantiotopic Selectivity of-Pig Liver Esterase Isoenzymes , 1990 .