Abstract This study evaluated the influence of temperature and β-galactosidase concentration on lactose hydrolysis and on the composition of pasteurized goat milk. Goat milk was pasteurized at 75 °C/15 s and cooled to 10 °C and 30 °C, received 0 (control); 0.04%; 0.07%; 0.20% (v/v) β-galactosidase and was incubated for 5 h, followed by enzymatic inactivation at 85 °C. The hydrolysis degree, pH and acidity were evaluated hourly. Physico-chemical parameters were determined after hydrolysis. The maximum hydrolysis degree (100%) has been reached in 4 h when using 0.07% and 0.20% lactase concentrations at 30 °C; however, the minimum hydrolysis percentage of 70% has been reached at 10 °C for all lactase concentrations tested since 1 h of incubation. The degree of hydrolysis and the total acidity of pasteurized goat milk increased with temperature. Low lactase concentrations resulted in an increase in protein levels, total casein, density, total and defatted dry extract. Therefore, combination of low lactase levels and hydrolysis at 10 °C promoted positive changes in lactose-free pasteurized goat milk. This study was the first reporting the changes resulting from enzymatic hydrolysis in the composition of pasteurized goat milk.

O isolado protéico das sementes de algaroba (Prosopis juliflora (SW) D.C.) foi modificado com anidrido acético nas concentrações de 5, 10, 20 e 30% (V/P), resultando, portanto, nos respectivos graus de modificação: 69,5; 83,2; 89,7 e 91,1% da lisina disponível. Caracterizou-se a funcionalidade do isolado nas formas não modificada e acetilada. O isolado não modificado apresentou alta solubilidade em pH ácido e básico, com exceção da faixa de pH 4 a 6. A acetilação deslocou o ponto isoelétrico das proteínas do pH 5 para o pH 4,5 , diminuiu em pequena extensão a solubilidade abaixo do ponto isoelétrico e aumentou a partir do pH 5, principalmente em pH 7. A capacidade de absorção de água e de óleo do isolado não modificado, que por sua vez se mostrou baixa (1,89 e 1,04g/g proteína), não melhorou satisfatoriamente após a modificação. O efeito de modificação nas propriedades espumantes foi maior com relação ao volume e a expansão da espuma formada do que na sua estabilidade. A capacidade emulsificante do isolado acetilado aumentou em grande extensão, no entanto, a atividade emulsificante e estabilidade de emulsão revelaram pequenos incrementos, em comparação com o isolado não modificado.

Protein isolate from seed of mesquite bean (P. juliflora (SW) D.C) were modified with acetic anhydride at concentrations 5, 10, 20 and 30% (ml per 100 g of protein) thus resulting 69.5; 83.2; 89.7 and 91.1% modification of available lysine. Functional characteristic of protein isolate was studied in native and acetilated form. Protein isolate in native form presented high solubility at acidic and basic pH, except in the pH range of 4 to 6. Acetilation shifted the isoelectric point of the proteins pH 5.0 to a pH 4.5; reduced the solubility at pH values below the isoelectric point and increased above pH 5.0, mainly at pH 7.0. The capacity of water and oil absorption of the native protein was small (1.89 and 1.04 g) and did not improve satisfactorily after modification. The effect of the modification on the foaming properties was higher in relation to the volume and foam expansion than its stability. Emulsifyng capacity of the acetylated protein isolate increased to the a higher extent, however, emulsifying activity and emulsion stability presented small variations in comparison to native protein isolate.