Caseinolytic and milk-clotting activities from Moringa oleifera flowers.
Food Chem
; 135(3): 1848-54, 2012 Dec 01.
Article
em En
| MEDLINE
| ID: mdl-22953932
This work reports the detection and characterization of caseinolytic and milk-clotting activities from Moringa oleifera flowers. Proteins extracted from flowers were precipitated with 60% ammonium sulphate. Caseinolytic activity of the precipitated protein fraction (PP) was assessed using azocasein, as well as α(s)-, ß- and κ-caseins as substrates. Milk-clotting activity was analysed using skim milk. The effects of heating (30-100°C) and pH (3.0-11.0) on enzyme activities were determined. Highest caseinolytic activity on azocasein was detected after previous incubation of PP at pH 4.0 and after heating at 50°C. Milk-clotting activity, detected only in the presence of CaCl(2), was highest at incubation of PP at pH 3.0 and remained stable up to 50°C. The pre-treatment of milk at 70°C resulted in highest clotting activity. Enzyme assays in presence of protease inhibitors indicated the presence of aspartic, cysteine, serine and metallo proteases. Aspartic proteases appear to be the main enzymes involved in milk-clotting activity. PP promoted extensive cleavage of κ-casein and low level of α(s)- and ß-caseins hydrolysis. The milk-clotting activity indicates the application of M. oleifera flowers in dairy industry.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Extratos Vegetais
/
Caseínas
/
Moringa oleifera
/
Flores
/
Leite
Limite:
Animals
Idioma:
En
Revista:
Food Chem
Ano de publicação:
2012
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Reino Unido