TY - JOUR
T1 - Enzymatic synthesis of N-acyl-L-amino acids in a glycerol-water system using acylase I from pig kidney
AU - Wada, Eiko
AU - Handa, Masato
AU - Imamura, Koreyoshi
AU - Sakiyama, Takaharu
AU - Adachi, Shuji
AU - Matsuno, Ryuichi
AU - Nakanishi, Kazuhiro
N1 - Funding Information:
This study was supported by the Program for Promotion of Basic Research Activities for Innovative Biosciences (PROBRAIN), Japan.
PY - 2002/1
Y1 - 2002/1
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.
KW - Acylase I
KW - Enzymatic synthesis
KW - N-acyl-L-amino acid
KW - Pig kidney
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U2 - 10.1007/s11746-002-0432-7
DO - 10.1007/s11746-002-0432-7
M3 - Article
AN - SCOPUS:0036193392
VL - 79
SP - 41
EP - 46
JO - Oil & Fat Industries
JF - Oil & Fat Industries
SN - 0003-021X
IS - 1
ER -