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Kinetically controlled enzymatic synthesis of dipeptide precursor of l ‐alanyl– l ‐glutamine
Author(s) -
Wang Mengfan,
Qi Wei,
Yu Qingxin,
Su Rongxin,
He Zhimin
Publication year - 2011
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.55
Subject(s) - dipeptide , chemistry , michaelis–menten kinetics , papain , nucleophile , yield (engineering) , biocatalysis , enzyme , glutamine , stereochemistry , peptide , peptide synthesis , reaction rate constant , protease , reaction mechanism , catalysis , organic chemistry , kinetics , amino acid , enzyme assay , biochemistry , materials science , physics , quantum mechanics , metallurgy
An important nutritional dipeptide precursor, benzoyloxycarbonyl protected l ‐alanyl– l ‐glutamine (Z–Ala–Gln), was successfully prepared through a kinetically controlled enzymatic peptide synthesis method. A commercially available and low‐cost protease (papain) was used as biocatalyst with Z–Ala–OMe and Gln as acyl donor and nucleophile, respectively. The dipeptide yield was 35.5% under the optimized reaction conditions: 35°C, pH 9.5, and the ratio of acyl donor/nucleophile is 1:10. Based on the reaction mechanism and experimental data, the kinetic model was established, which was in accordance with the Michaelis–Menten equation, and the apparent Michaelis constant K m appand the apparent maximum reaction rate r max appwere calculated as 1.71 mol/L and 6.09 mmol/(L Min), respectively.