“…Dairy proteins have DIAAS that are greater than plant proteins (3,4) . Other animal proteins, such as fish and animal protein hydrolysates, have greater DIAAS than plant proteins (5,6) , and the DIAAS of beef was recently determined to be greater than that in plant proteins (7) . Meat is a concentrated source of protein providing a balanced indispensable AA (IAA) pattern in diets for humans, and in most cases, meat is further processed prior to consumption (8) .…”
An experiment was conducted to test the hypothesis that meat products have digestible indispensable amino acid scores (DIAAS) >100 and that various processing methods will increase standardised ileal digestibility (SID) of amino acids (AA) and DIAAS. Nine ileal-cannulated gilts were randomly allotted to a 9 × 8 Youden square design with nine diets and eight 7-d periods. Values for SID of AA and DIAAS for two reference patterns were calculated for salami, bologna, beef jerky, raw ground beef, cooked ground beef and ribeye roast heated to 56, 64 or 72°C. The SID of most AA was not different among salami, bologna, beef jerky and cooked ground beef, but was less (P < 0·05) than the values for raw ground beef. The SID of AA for 56°C ribeye roast was not different from the values for raw ground beef and 72°C ribeye roast, but greater (P < 0·05) than those for 64°C ribeye roast. For older children, adolescents and adults, the DIAAS for all proteins, except cooked ground beef, were >100 and bologna and 64°C ribeye roast had the greatest (P < 0·05) DIAAS. The limiting AA for this age group were sulphur AA (beef jerky), leucine (bologna, raw ground beef and cooked ground beef) and valine (salami and the three ribeye roasts). In conclusion, meat products generally provide high-quality protein with DIAAS >100 regardless of processing. However, overcooking meat may reduce AA digestibility and DIAAS.
“…Dairy proteins have DIAAS that are greater than plant proteins (3,4) . Other animal proteins, such as fish and animal protein hydrolysates, have greater DIAAS than plant proteins (5,6) , and the DIAAS of beef was recently determined to be greater than that in plant proteins (7) . Meat is a concentrated source of protein providing a balanced indispensable AA (IAA) pattern in diets for humans, and in most cases, meat is further processed prior to consumption (8) .…”
An experiment was conducted to test the hypothesis that meat products have digestible indispensable amino acid scores (DIAAS) >100 and that various processing methods will increase standardised ileal digestibility (SID) of amino acids (AA) and DIAAS. Nine ileal-cannulated gilts were randomly allotted to a 9 × 8 Youden square design with nine diets and eight 7-d periods. Values for SID of AA and DIAAS for two reference patterns were calculated for salami, bologna, beef jerky, raw ground beef, cooked ground beef and ribeye roast heated to 56, 64 or 72°C. The SID of most AA was not different among salami, bologna, beef jerky and cooked ground beef, but was less (P < 0·05) than the values for raw ground beef. The SID of AA for 56°C ribeye roast was not different from the values for raw ground beef and 72°C ribeye roast, but greater (P < 0·05) than those for 64°C ribeye roast. For older children, adolescents and adults, the DIAAS for all proteins, except cooked ground beef, were >100 and bologna and 64°C ribeye roast had the greatest (P < 0·05) DIAAS. The limiting AA for this age group were sulphur AA (beef jerky), leucine (bologna, raw ground beef and cooked ground beef) and valine (salami and the three ribeye roasts). In conclusion, meat products generally provide high-quality protein with DIAAS >100 regardless of processing. However, overcooking meat may reduce AA digestibility and DIAAS.
“…Therefore, PBM HA derived from raw material rich in collagen ( Pérez-Calvo et al, 2010 ) such as high amounts of muscle tissue (mechanically separated meat) and bone waste had greater digestibility (CI 82.01–84.30%) than PBM LA (CI 79.52–81.02%). Although collagen has a low biological value due to its lower content of essential amino acids, its digestibility is high ( Bindari et al, 2018 ), unlike in PBM LA , in which contains by-products derived from the organs and intestines with lower digestibility, but with a better amino acid profile.…”
“…The crystalline AA diet was based on the AA profile of casein with glutamic acid and proline used to substitute the crude protein (CP) contribution of the AA not available as crystalline AA (Cys, Arg, Asp, Ser). The experimental diets were formulated with the aim of being iso-nitrogenous (200 g CP/kg as-fed basis) by diluting the protein sources with nitrogen-free ingredients [ 15 ], except for wheat, which contained less than 200 g CP/kg (as-fed) and, therefore, fed without dilution. The ingredient composition of the seven experimental diets is presented in Table 1 , the AA content of the protein sources in Table 2 , and the analyzed chemical composition of the diets is presented in Table 3 .…”
The aim of the present study was to determine postprandial amino acid (AA) appearance in the blood of growing pigs as influenced by protein source. Seven growing pigs (average body weight 18 kg), in a 7 × 5 Youden square design, were fitted with a jugular vein catheter and fed seven diets containing wheat, soybean meal, enzyme-treated soybean meal, hydrothermally-treated rapeseed meal, casein, hydrolyzed casein, and a crystalline AA blend with the same AA profile as casein. The latter was not eaten by the pigs, therefore being excluded. Blood samples were collected at −30, 30, 60, 90, 120, 180, and 360 min after a meal and analyzed for free AA. Overall, plasma AA concentrations were highest 60 min after feeding. There were no differences in plasma AA concentration between casein and hydrolyzed casein, but soybean meal resulted in lower AA plasma concentrations compared with enzyme-treated soybean meal at 60 and 120 min after feeding. There were no differences between hydrothermally-treated rapeseed meal and soybean meal. In conclusion, the ingredients could not clearly be categorized as being slow or fast protein with regard to protein digestion and absorption of AA, but soybean meal resulted in a prolonged appearance of plasma AA compared to casein and hydrolyzed casein.
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