The thermo-active serine peptidase aqualysin 1 (Aq1) of Thermus aquaticus was applied in bread making to study the relative contribution of thermoset gluten to bread crumb texture. Aq1 is active between 30 °C and 90 °C with an optimum activity temperature of around 65 °C. It is inhibited by wheat endogenous serine peptidase inhibitors during dough ...
Published in ACS chemical biology
The elucidation of protein/drug interactions remains a major challenge in drug discovery. Liquid chromatography-tandem mass spectrometry has emerged as a tremendously powerful technology for this endeavor, but its full potential has yet to be realized owing in part to unresolved challenges in data analysis. Herein, we demonstrate how tandem mass sp...
Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES), Brazil
Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES), Brazil
Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES), Brazil
Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES), Brazil
Published in Acta crystallographica. Section D, Biological crystallography
Previous studies have shown that the trypsin inhibitors LMPI-1, LMPI-3 and SGTI from locusts display an unusual species selectivity. They inhibit locust, crayfish and fungal trypsins several orders of magnitude more efficiently than bovine trypsin. In contrast, the chymotrypsin inhibitors from the same family, LMPI-2 and SGCI, are active towards ma...
Three experimental diets in which fish meal was partially (50 and 75%, named PP50 and PP75 diets, respectively) or totally replaced (PP100 diet) by plant protein sources were fed to rainbow trout and gilthead sea bream. We studied the effects of these diets on digestive enzymes in Comparison to fish fed fish meal diets (FM). A mixture of vegetal in...
As differences in protein composition between camel and bovine milk may influence their digestibility, hydrolysis of milk proteins of both species using two pancreatic serine proteases (trypsin and chymotrypsin) was studied. Caseins (CNs) were more rapidly hydrolyzed than whey proteins (WPs) because of their greater flexibility and open structures....
