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

15 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
Publication statusPublished - Jan 2002

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Glycerol
Amino acids
glycerol
Swine
kidneys
Kidney
Amino Acids
swine
amino acids
glutamic acid
synthesis
Water
Glutamic Acid
Arginine
Acids
Fatty acids
water
arginine
Fatty Acids
Enzymes

Keywords

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

ASJC Scopus subject areas

  • Food Science
  • Chemistry (miscellaneous)

Cite this

Enzymatic synthesis of N-acyl-L-amino acids in a glycerol-water system using acylase I from pig kidney. / Wada, Eiko; Handa, Masato; Imamura, Koreyoshi; Sakiyama, Takaharu; Adachi, Shuji; Matsuno, Ryuichi; Nakanishi, Kazuhiro.

In: JAOCS, Journal of the American Oil Chemists' Society, Vol. 79, No. 1, 01.2002, p. 41-46.

Research output: Contribution to journalArticle

Wada, Eiko ; Handa, Masato ; Imamura, Koreyoshi ; Sakiyama, Takaharu ; Adachi, Shuji ; Matsuno, Ryuichi ; Nakanishi, Kazuhiro. / Enzymatic synthesis of N-acyl-L-amino acids in a glycerol-water system using acylase I from pig kidney. In: JAOCS, Journal of the American Oil Chemists' Society. 2002 ; Vol. 79, No. 1. pp. 41-46.
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AU - Adachi, Shuji

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AU - Nakanishi, Kazuhiro

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N2 - 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.

AB - 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.

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