Synthesis of delicious peptide fragments catalyzed by immobilized proteases

M. D. Romero; J. Aguado; M. J. Guerra; G. Alvaro; R. Navarro; E. Rubio

Synthesis of delicious peptide fragments catalyzed by immobilized proteases

M. D. Romero, J. Aguado, M. J. Guerra, G. Alvaro, R. Navarro, E. Rubio

Research output: Contribution to journal › Article › Research › peer-review

Abstract

The synthesis of benzyloxycarbonyl-lysine-glycine methyl ester (CBZ-Lys-Gly-OMe) and benzyloxycarbonyl-serine-leucine methyl ester (CBZ-Ser-Leu-OMe) have been carried out in aqueous organic systems catalyzed by immobilized trypsin and thermolysin respectively. The dipeptides originated by the elimination of benzyloxycarbonyl and methoxy groups are two fragments of the delicious peptide, which is an octapeptide of industrial interest with a taste profile umami/sour. In both synthesis we have studied the influence of pH, temperature and substrate concentration on the yield and the rate of synthesis. In the optimum conditions, the synthetic yields were 80% for CBZ-Lys-Gly-OMe and 100% for CBZ-Ser-Leu-OMe. Both synthesis present an inhibition effect by the acyl donor when the concentrations of CBZ-Lys and CBZ-Ser are higher than 20 mM. In the synthesis of CBZ-Ser-Leu-OMe an anomalous role of thermolysin has been observed forming oligopeptides of higher molecular weight by addition of new molecules of aminoacid Leu-OMe. © 1997 Elsevier Science B.V. All rights reserved.

Original language	English
Pages (from-to)	657-664
Journal	Studies in Surface Science and Catalysis
Volume	108
Publication status	Published - 1 Jan 1997

Cite this

@article{875c5d14a3f54bdeafb642231671bd65,

title = "Synthesis of delicious peptide fragments catalyzed by immobilized proteases",

abstract = "The synthesis of benzyloxycarbonyl-lysine-glycine methyl ester (CBZ-Lys-Gly-OMe) and benzyloxycarbonyl-serine-leucine methyl ester (CBZ-Ser-Leu-OMe) have been carried out in aqueous organic systems catalyzed by immobilized trypsin and thermolysin respectively. The dipeptides originated by the elimination of benzyloxycarbonyl and methoxy groups are two fragments of the delicious peptide, which is an octapeptide of industrial interest with a taste profile umami/sour. In both synthesis we have studied the influence of pH, temperature and substrate concentration on the yield and the rate of synthesis. In the optimum conditions, the synthetic yields were 80% for CBZ-Lys-Gly-OMe and 100% for CBZ-Ser-Leu-OMe. Both synthesis present an inhibition effect by the acyl donor when the concentrations of CBZ-Lys and CBZ-Ser are higher than 20 mM. In the synthesis of CBZ-Ser-Leu-OMe an anomalous role of thermolysin has been observed forming oligopeptides of higher molecular weight by addition of new molecules of aminoacid Leu-OMe. {\textcopyright} 1997 Elsevier Science B.V. All rights reserved.",

author = "Romero, {M. D.} and J. Aguado and Guerra, {M. J.} and G. Alvaro and R. Navarro and E. Rubio",

year = "1997",

month = jan,

day = "1",

language = "English",

volume = "108",

pages = "657--664",

}

TY - JOUR

T1 - Synthesis of delicious peptide fragments catalyzed by immobilized proteases

AU - Romero, M. D.

AU - Aguado, J.

AU - Guerra, M. J.

AU - Alvaro, G.

AU - Navarro, R.

AU - Rubio, E.

PY - 1997/1/1

Y1 - 1997/1/1

N2 - The synthesis of benzyloxycarbonyl-lysine-glycine methyl ester (CBZ-Lys-Gly-OMe) and benzyloxycarbonyl-serine-leucine methyl ester (CBZ-Ser-Leu-OMe) have been carried out in aqueous organic systems catalyzed by immobilized trypsin and thermolysin respectively. The dipeptides originated by the elimination of benzyloxycarbonyl and methoxy groups are two fragments of the delicious peptide, which is an octapeptide of industrial interest with a taste profile umami/sour. In both synthesis we have studied the influence of pH, temperature and substrate concentration on the yield and the rate of synthesis. In the optimum conditions, the synthetic yields were 80% for CBZ-Lys-Gly-OMe and 100% for CBZ-Ser-Leu-OMe. Both synthesis present an inhibition effect by the acyl donor when the concentrations of CBZ-Lys and CBZ-Ser are higher than 20 mM. In the synthesis of CBZ-Ser-Leu-OMe an anomalous role of thermolysin has been observed forming oligopeptides of higher molecular weight by addition of new molecules of aminoacid Leu-OMe. © 1997 Elsevier Science B.V. All rights reserved.

AB - The synthesis of benzyloxycarbonyl-lysine-glycine methyl ester (CBZ-Lys-Gly-OMe) and benzyloxycarbonyl-serine-leucine methyl ester (CBZ-Ser-Leu-OMe) have been carried out in aqueous organic systems catalyzed by immobilized trypsin and thermolysin respectively. The dipeptides originated by the elimination of benzyloxycarbonyl and methoxy groups are two fragments of the delicious peptide, which is an octapeptide of industrial interest with a taste profile umami/sour. In both synthesis we have studied the influence of pH, temperature and substrate concentration on the yield and the rate of synthesis. In the optimum conditions, the synthetic yields were 80% for CBZ-Lys-Gly-OMe and 100% for CBZ-Ser-Leu-OMe. Both synthesis present an inhibition effect by the acyl donor when the concentrations of CBZ-Lys and CBZ-Ser are higher than 20 mM. In the synthesis of CBZ-Ser-Leu-OMe an anomalous role of thermolysin has been observed forming oligopeptides of higher molecular weight by addition of new molecules of aminoacid Leu-OMe. © 1997 Elsevier Science B.V. All rights reserved.

M3 - Article

VL - 108

SP - 657

EP - 664

ER -

Synthesis of delicious peptide fragments catalyzed by immobilized proteases

Abstract

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