Variation in seed protein digestion of different pea (Pisum sativum L.) genotypes by cecectomized broiler chickens: 2. Relation between in vivo protein digestibility and pea seed characteristics, and identification of resistant pea polypeptides

Relationship between proportion and composition of albumins, and in vitro protein digestibility of raw and cooked pea seeds (Pisum sativum L.)

“…In globulin fractions, increased intensities of legumin α (∼45 kDa) and legumin β (∼25–29 kDa) were observed as seed protein content increased in seven smooth pea varieties ( r = 0.933, P < 0.01 and r = 0.743, P < 0.05, respectively) (Fig. 1(B) and Table 3) as reported proviously 3, 21. Windham and Spector, which had much lower seed protein content than other pea varieties, exhibited greater intensities of vicilin (around 50 kDa) and matured vicilin (around 35 kDa), indicating the possible association of the quantity of those proteins with seed protein content.…”

“…Although thermal treatment could inactivate the antinutritional function of those albumin proteins, their digestibility is not improved in peas, chickpeas, or dry beans 11, 12, 15 . In vivo protein digestibility studies using various animals have indicated that pea albumins (PA2 and PA1) and lectins are the commonly detected protease‐resistant polypeptides in peas and chickpeas 14, 16, 17, 20, 21. Proteolytic resistance of those albumins are caused by compact structure involving disulfide bonds in protease inhibitors and PA25 and rich β‐sheet structures in lectins 22…”

Effects of including raw or extruded field peas (Pisum sativum L.) in diets fed to weanling pigs

“…The presence of anti-nutritional factors in field peas is well documented, 11,12 and some of these anti-nutritional factors may be inactivated if heated. To investigate whether thermal treatment might alleviate the negative effects of including 480 g kg −1 raw field peas in diets fed to weanling pigs as observed in Experiment 1, field peas were extruded to reduce a possible negative impact of anti-nutritional factors in the peas.…”

Variation in seed protein digestion of different pea (Pisum sativum L.) genotypes by cecectomized broiler chickens: 1. Endogenous amino acid losses, true digestibility and in vitro hydrolysis of proteins

“…These differences can partly be explained by the differences in endogenous losses as well as by the differences in true digestibility of pea proteins. These differences between pea genotypes were studied in relation to seed composition and particularly to the seed protein composition (Gabriel et al, 2007).…”