Lipase-catalyzed enantioselective hydrolysis of N-protected racemic non-protein amino acid esters

Ken Ichi Kagawa, Teruhiko Matsubara, Katsuhiro Kawashiro

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Porcine pancreatic lipase (PPL)-catalyzed enantioselective hydrolysis of N-benzyloxycarbonyl-dl-amino acid esters (Z-dl-AA-ORs) was studied for the optical resolution of a variety of non-protein amino acids. The ester moiety (R) of the substrate affected the rate of hydrolysis significantly. The glyceryl (Gl) and carbamoylmethyl (Cam) esters were found to be highly reactive substrates. The hydrolysis of the Gl esters (Z-dl-AA-OGls) of both aliphatic and aromatic amino acids was examined in acetonitrile containing 70% (v/v) of 0.02 M phosphate buffer (pH 7.0) at 30°C. With all amino acids tested, the corresponding l-enantiomers were hydrolyzed preferentially. PPL favored aromatic amino acids, such as phenylalanine and p-chlorophenylalanine, leading to completion of the hydrolysis within 20 min with excellent enantioselectivities (E>100). The PPL-catalyzed hydrolysis of the corresponding Cam esters (Z-dl-AA-OCams) was also examined under the same reaction conditions. Although the hydrolysis of the Cam esters was rapid, the l-enantioselectivities were rather poor with aromatic amino acids, such as 2-phenylglycine and homophenylalanine.

Original languageEnglish
Pages (from-to)186-196
Number of pages11
JournalBiocatalysis and Biotransformation
Volume26
Issue number3
DOIs
Publication statusPublished - 2008 Jul

Fingerprint

Lipases
Lipase
Amino acids
Hydrolysis
Esters
Amino Acids
Aromatic Amino Acids
Carboxylic acids
Swine
Enantioselectivity
Fenclonine
Enantiomers
Substrates
Acetonitrile
Phenylalanine
Buffers
Phosphates

Keywords

  • Carbamoylmethyl ester
  • Enantio selective hydrolysis
  • Glyceryl ester
  • Non-protein amino acid
  • Optical resolution
  • Porcine pancreatic lipase

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biotechnology
  • Catalysis

Cite this

Lipase-catalyzed enantioselective hydrolysis of N-protected racemic non-protein amino acid esters. / Kagawa, Ken Ichi; Matsubara, Teruhiko; Kawashiro, Katsuhiro.

In: Biocatalysis and Biotransformation, Vol. 26, No. 3, 07.2008, p. 186-196.

Research output: Contribution to journalArticle

@article{aac2876995f74e0eada1240dfd4a5f49,
title = "Lipase-catalyzed enantioselective hydrolysis of N-protected racemic non-protein amino acid esters",
abstract = "Porcine pancreatic lipase (PPL)-catalyzed enantioselective hydrolysis of N-benzyloxycarbonyl-dl-amino acid esters (Z-dl-AA-ORs) was studied for the optical resolution of a variety of non-protein amino acids. The ester moiety (R) of the substrate affected the rate of hydrolysis significantly. The glyceryl (Gl) and carbamoylmethyl (Cam) esters were found to be highly reactive substrates. The hydrolysis of the Gl esters (Z-dl-AA-OGls) of both aliphatic and aromatic amino acids was examined in acetonitrile containing 70{\%} (v/v) of 0.02 M phosphate buffer (pH 7.0) at 30°C. With all amino acids tested, the corresponding l-enantiomers were hydrolyzed preferentially. PPL favored aromatic amino acids, such as phenylalanine and p-chlorophenylalanine, leading to completion of the hydrolysis within 20 min with excellent enantioselectivities (E>100). The PPL-catalyzed hydrolysis of the corresponding Cam esters (Z-dl-AA-OCams) was also examined under the same reaction conditions. Although the hydrolysis of the Cam esters was rapid, the l-enantioselectivities were rather poor with aromatic amino acids, such as 2-phenylglycine and homophenylalanine.",
keywords = "Carbamoylmethyl ester, Enantio selective hydrolysis, Glyceryl ester, Non-protein amino acid, Optical resolution, Porcine pancreatic lipase",
author = "Kagawa, {Ken Ichi} and Teruhiko Matsubara and Katsuhiro Kawashiro",
year = "2008",
month = "7",
doi = "10.1080/10242420701568641",
language = "English",
volume = "26",
pages = "186--196",
journal = "Biocatalysis and Biotransformation",
issn = "1024-2422",
publisher = "Informa Healthcare",
number = "3",

}

TY - JOUR

T1 - Lipase-catalyzed enantioselective hydrolysis of N-protected racemic non-protein amino acid esters

AU - Kagawa, Ken Ichi

AU - Matsubara, Teruhiko

AU - Kawashiro, Katsuhiro

PY - 2008/7

Y1 - 2008/7

N2 - Porcine pancreatic lipase (PPL)-catalyzed enantioselective hydrolysis of N-benzyloxycarbonyl-dl-amino acid esters (Z-dl-AA-ORs) was studied for the optical resolution of a variety of non-protein amino acids. The ester moiety (R) of the substrate affected the rate of hydrolysis significantly. The glyceryl (Gl) and carbamoylmethyl (Cam) esters were found to be highly reactive substrates. The hydrolysis of the Gl esters (Z-dl-AA-OGls) of both aliphatic and aromatic amino acids was examined in acetonitrile containing 70% (v/v) of 0.02 M phosphate buffer (pH 7.0) at 30°C. With all amino acids tested, the corresponding l-enantiomers were hydrolyzed preferentially. PPL favored aromatic amino acids, such as phenylalanine and p-chlorophenylalanine, leading to completion of the hydrolysis within 20 min with excellent enantioselectivities (E>100). The PPL-catalyzed hydrolysis of the corresponding Cam esters (Z-dl-AA-OCams) was also examined under the same reaction conditions. Although the hydrolysis of the Cam esters was rapid, the l-enantioselectivities were rather poor with aromatic amino acids, such as 2-phenylglycine and homophenylalanine.

AB - Porcine pancreatic lipase (PPL)-catalyzed enantioselective hydrolysis of N-benzyloxycarbonyl-dl-amino acid esters (Z-dl-AA-ORs) was studied for the optical resolution of a variety of non-protein amino acids. The ester moiety (R) of the substrate affected the rate of hydrolysis significantly. The glyceryl (Gl) and carbamoylmethyl (Cam) esters were found to be highly reactive substrates. The hydrolysis of the Gl esters (Z-dl-AA-OGls) of both aliphatic and aromatic amino acids was examined in acetonitrile containing 70% (v/v) of 0.02 M phosphate buffer (pH 7.0) at 30°C. With all amino acids tested, the corresponding l-enantiomers were hydrolyzed preferentially. PPL favored aromatic amino acids, such as phenylalanine and p-chlorophenylalanine, leading to completion of the hydrolysis within 20 min with excellent enantioselectivities (E>100). The PPL-catalyzed hydrolysis of the corresponding Cam esters (Z-dl-AA-OCams) was also examined under the same reaction conditions. Although the hydrolysis of the Cam esters was rapid, the l-enantioselectivities were rather poor with aromatic amino acids, such as 2-phenylglycine and homophenylalanine.

KW - Carbamoylmethyl ester

KW - Enantio selective hydrolysis

KW - Glyceryl ester

KW - Non-protein amino acid

KW - Optical resolution

KW - Porcine pancreatic lipase

UR - http://www.scopus.com/inward/record.url?scp=42049102423&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=42049102423&partnerID=8YFLogxK

U2 - 10.1080/10242420701568641

DO - 10.1080/10242420701568641

M3 - Article

AN - SCOPUS:42049102423

VL - 26

SP - 186

EP - 196

JO - Biocatalysis and Biotransformation

JF - Biocatalysis and Biotransformation

SN - 1024-2422

IS - 3

ER -