To what extent does the nitrosation of meat proteins influence their digestibility?

Cooking does not impair the impact of pulsed electric field on the protein digestion of venison (Cervus elaphus) during in vitro gastrointestinal digestion

“…The proteins are broken down to free amino acids or smaller peptides with few amino acid residues, such as tetrapeptides, tripeptides and dipeptides during digestion (Pappenheimer et al ., 1994; Jahan‐Mihan et al ., 2011). Non‐thermal processes which can alter the structure of a protein can modify the accessibility of gastrointestinal enzymes to the cleavage sites on proteins and can affect the rate and extend of hydrolysis during digestion (Yu, Morton, Clerens, & Dyer, 2017; Thérona et al ., 2018; Bhat et al ., 2018a). Denaturation induces unfolding of proteins and can make them more flexible and open, and this can influence the hydrolysis of protein substrates by affecting their interaction with active site of proteases (Yu, Morton, Clerens, & Dyer, 2017).…”

Controlar os parâmetros de assamento (tempo, temperatura, umidade) pode permitir a melhoria de algumas propriedades físicas e nutricionais de pães

“…A qualidade nutricional das proteínas está relacionada com os peptídeos de cadeia curta formados durante o processo de digestão (KETNAWA; OGAWA, 2019). A hidrólise da proteína irá formar peptídeos e aminoácidos, que por sua vez irão contribuir para deixar o nitrato mais disponível (THÉRON et al, 2018). Portanto, um aumento na digestibilidade implicará em um aumento na qualidade proteica (KETNAWA; OGAWA, 2019).…”