Organic reactions catalyzed by insolubilized enzymes; i-peptide synthesis catalyzed by insolubilized α-chymotrypsin
1990; Science Press; Volume: 62; Issue: 1 Linguagem: Inglês
10.1016/0304-5102(90)85243-b
ISSN1873-3131
AutoresDomingo Martín Salvador, J.V. Sinisterra, José M. Guisán,
Tópico(s)RNA and protein synthesis mechanisms
ResumoAbstract The synthesis of several peptidic bonds (Tyr-Leu, Tyr-Gly and Tyr-Ala) was carried out in organic-aqueous media under kinetically controlled conditions. Insolubilized α-chymotrypsin on agarose was used as catalyst. A 60%–70% yield in peptide was obtained using 20% DMF, pH = 10 and temperature 25 °C. The influence of several organic solvents in the catalytic activity of the enzyme was analyzed. The influence of the pH was studied. pH>8 favours the synthesis of peptide. The nature of the nucleophile (L-Leu, Gly or L-Ala) does not seem to any great extent to affect the yield in peptide at constant reaction time. From these data a more detailed mechanism of the enzymatic activity is proposed.
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