RESUMO
Whey is a cheese co-product with high protein content used in the food industry due to its techno-functional properties and nutritive value. This study aims to optimize the production of ß-lactoglobulin (ß-lg) nanostructures, to characterize their techno-functional properties and stability, and to apply them as a carrier of bioactive molecules. Box-Behnken planning was applied to determine the best conditions to obtain the ß-lg nanostructure, which consists in treatment at 100 °C in NaCl 50 mmol·L-1 for 60 min. TEM analysis showed a fibril structure in the observed nanostructures. The nanostructured systems formed foam and emulsion with higher stability than the systems composed of the native protein. The results for encapsulation efficiency of bioactive compounds were 96.50%, 89.04%, 67.78%, and 36.39% for quercetin, rutin, naringin, and vitamin B2, respectively. Thus, ß-lg nanostructure's great capacity to encapsulate hydrophobic molecules was verified.
Assuntos
Lactoglobulinas/química , Nanoestruturas/química , Cápsulas , Queijo , Interações Hidrofóbicas e HidrofílicasRESUMO
Aprotinin, the most studied serine proteinase inhibitor, was isolated from porcine lung for the first time. The purified porcine aprotinin had an Mr value of approximately 7 kDa. It cross-reacted with polyclonal serum anti-commercial aprotinin. About 1 microg porcine aprotinin inhibited 6 microg trypsin whereas 1 microg commercial soybean inhibitor inhibited only 1 microg trypsin. The aprotinin gene was also isolated from porcine lung: the deduced amino acid sequence showed 74% identity to bovine aprotinin.
