Enzymatic synthesis of N-acyl-L-amino acids in a glycerol-water system using acylase I from pig kidney

Eiko Wada, Masato Handa, Koreyoshi Imamura, Takaharu Sakiyama, Shuji Adachi, Ryuichi Matsuno, Kazuhiro Nakanishi

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

N-Medium-and long-chain acyl-L-amino acids were enzymatically synthesized from the corresponding L-amino acids and fatty acids using a reverse hydrolysis. Enzymes that are suitable for the synthetic reaction of N-acyl-L-amino acids were screened on the basis of hydrolytic activity toward N-lauroyl-L-glutamic acid as an indicator. Acylase I from pig kidney (EC 3.5.1.14) showed the highest N-acyl-L-amino acid hydrolytic activity among 57 commercially available enzymes tested. Acylase I effectively catalyzed the synthesis of N-lauroyl-L-amino acids except for N-lauroyl-L-proline and N-lauroyl-L-tyrosine in a glycerol-water system. Under the optimized reaction conditions, N-lauroyl-L-arginine and N-lauroyl-L-glutamic acid were obtained in conversions of 82 and 44%, respectively. The equilibrium constants calculated from the conversion obtained were 5.6, 15.4, 18.0, and 39.4 for the syntheses of N-lauroyl-L-glutamic acid, Nα-lauroyl-L-lysine, N-lauroyl-L-glutamine, and N-lauroyl-L-methionine, respectively. N-Acyl-L-arginines with myristic acid and palmitic acid as the fatty acid were also synthesized using acylase I.

Original languageEnglish
Pages (from-to)41-46
Number of pages6
JournalJAOCS, Journal of the American Oil Chemists' Society
Volume79
Issue number1
DOIs
Publication statusPublished - Jan 2002

Keywords

  • Acylase I
  • Enzymatic synthesis
  • N-acyl-L-amino acid
  • Pig kidney

ASJC Scopus subject areas

  • Chemical Engineering(all)
  • Organic Chemistry

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