RESUMO
Effects of gamma irradiation at doses of 1 kGy, 5 kGy, and 10 kGy on water absorption properties, cooking quality and electrophoretic patterns of insoluble proteins of red and green lentil samples were investigated. The densitometric analysis indicated that the effects of irradiation on sodium dodecyl sulfate-polycrylamide gel electrophoresis patterns of red and green lentil proteins were not significant. Generally, a 1 kGy irradiation dose did not significantly affect the water absorption properties of the lentil samples while significant increases were observed at the 5 kGy level. The dry and wet cooking times were found to be significantly decreased, as the irradiation level increased in all red and green lentil samples.
Assuntos
Proteínas Alimentares/efeitos da radiação , Lens (Planta)/efeitos da radiação , Água/fisiologia , Absorção , Eletroforese em Gel de Poliacrilamida/métodos , Irradiação de Alimentos , Conservação de Alimentos/métodos , Raios gama , Temperatura Alta , Lens (Planta)/fisiologia , Cloreto de Sódio/metabolismo , SolubilidadeRESUMO
The contribution of the three-dimensional structures of one heptapeptide (PQPQPFP) sequence and one pentapeptide (PQQPY) repeat sequence of alpha/beta-gliadins, one heptapeptide (PQQPFPQ) repeat sequence of gamma-gliadins, two heptapeptide (PQQPPFS and QQQQPVL) repeat motifs of low-molecular-weight (LMW) subunits and a tetrapeptide sequence in polyQ region of S-rich prolamins to their conformations are investigated by using the recently developed multicanonical simulation procedure. Ramachandran plots were prepared and analysed to predict the relative occurrence probabilities of gamma-tutn, gamma-turn, and helical structures. The probability of inverse 7-turn was generally higher than that of beta-turns in all sequences investigated. Occurrence probability of helical structure in the repetitive domain of gliadins was low. Structural predictions of QQQQPVL sequence of LMW-glutenin subunits and QQQQ sequence in the polyQ region of S-rich prolamins indicate the presence of helical structures with the probability of >20%. The probability of helical structure significantly decreased around 100 degrees C.