Lysozyme precipitation induced by the addition of the volatile salt ammonium carbamate was studied through cloud-point measurements and precipitation assays. Phase equilibrium experiments were carried out at 5.0, 15.0 and 25.0 °C and the compositions of the coexisting phases were determined. A...

Lysozyme precipitation induced by the addition of the volatile salt ammonium carbamate was studied through cloud-point measurements and precipitation assays. Phase equilibrium experiments were carried out at 5.0, 15.0 and 25.0 °C and the compositions of the coexisting phases were determined. A complete separation of the coexisting liquid and solid phases could not be achieved. Nevertheless it was possible to determine the composition of the solid precipitate through the extensions of experimental tie lines. The same precipitate was found at all temperatures. Lysozyme enzymatic activities of the supernatant and precipitate phases were also determined. The activity balance suggests that ammonium carbamate preserves lysozyme activity after the salting-out precipitation

FUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULO - FAPESP

COORDENAÇÃO DE APERFEIÇOAMENTO DE PESSOAL DE NÍVEL SUPERIOR - CAPES

CONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICO - CNPQ

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