Trypsin inhibitors (
TI
) resident in soybeans affects protein utilization. While heat treatment influences residual TI, it simultaneously affects the structure and solubility of the soybean proteins and confounds any response to exogenous proteases. Using purified TI, the effect of exogenous protease to TI can be dissociated from changes in the soybean protein. Thus, the current study was designed to evaluate the growth performance and protein utilization responses of broiler chickens to purified TI and exogenous protease. Soybean meal (
SBM
) was preanalyzed for basal TI (2,996 TIU/g SBM), formulated into nutritionally adequate experimental diets to contain 1,033 TIU/g diet, and purified TI was added at 9,000 TIU/g diet. A total of 320 Cobb-500 broiler chicks were allocated to 4 diets, each with 8 replicate cages and 10 birds per replicate. The experimental diets were arranged as a 2 × 2 factorial with factors being dietary TI (1,033 or 10,033 TIU/g) and exogenous protease (0 or 15,000 PROT/kg). On day 7, 14, and 21 posthatching, protease supplementation improved the BW gain (
P
< 0.01) and gain to feed ratio (
P
< 0.05) of birds. On day 14 and 21 posthatching, the relative weight of pancreas increased (
P
< 0.05) with added TI but was reduced (
P
< 0.001) with protease supplementation. Apparent ileal digestibility of all amino acids, except methionine, decreased (
P
< 0.001) with added TI but increased (
P
< 0.05) with protease supplementation. Jejunal MUC-2 was downregulated (
P
< 0.01) and SCL7A-2 was upregulated (
P
< 0.05) by protease supplementation. Duodenal trypsin and chymotrypsin activities reduced (
P
< 0.05) with added TI but increased
(P
< 0.01) with protease supplementation. Exogenous protease produced longer villi (
P
< 0.05) and deeper crypts (
P
< 0.01) in the jejunal tissue. In conclusion, dietary addition of purified TI negatively affects nutrient utilization by broiler chickens. Furthermore, the study showed that the efficacy of the exogenous protease might be independent of dietary TI concentration.
Two experiments were conducted to determine the effects of protease supplementation on degradation of soybean meal (SBM) allergenic proteins (glycinin and β-conglycinin) and gut health of weaned pigs fed soybean meal-based diets. In Experiment 1, two SBM samples from 2 different sources were subjected to porcine in vitro gastric degradation to determine the effects of protease (at 15,000 U/kg of feedstuff) on degradation of the soybean allergenic proteins. In Experiment 2, forty-eight weaned pigs (body weight = 6.66 kg) were obtained in 2 batches of 24 pigs each. Pigs were individually housed in metabolic crates and fed 4 diets (12 pigs/diet). The diets were corn-based diet with SBM 1 or SBM 2 without or with protease at 15,000 U/kg of diet in 2 × 2 factorial arrangement. Diets were fed for 10 d and pigs were sacrificed on d 10 for measurement of small intestinal histomorphology, permeability of small intestine mounted in Ussing chambers, and serum concentration of pro-inflammatory cytokines. Two SBM sources (SBM 1 and SBM 2) contained 46.9 or 47.7% CP, 14.0 or 14.6% glycinin, and 9.90 or 10.3% β-conglycinin, respectively. Protease and SBM source did not interact on any of the response criteria measured in the current study. Protease supplementation tended to increase (P = 0.069) the in vitro gastric degradation of glycinin. Protease supplementation tended to reduce (P = 0.099) fluorescein isothiocyanate dextran 4,000 Da (which is a marker probe for intestinal permeability) flow in jejunum, and reduced (P = 0.037) serum TNF-α concentration. Protease did not affect small intestinal histomorphology. In conclusion, protease tended to increase gastric degradation of glycinin, and reduce gut permeability, and serum concentration of pro-inflammatory cytokines, indicating that the protease used in the current study can be added to SBM-based diets for weanling pigs to improve gut health.
Two experiments were conducted to determine the effects of protease supplementation on degradation of soybean meal (SBM) allergenic proteins (glycinin and β-conglycinin) and gut health of weaned pigs fed SBM-based diets. In Experiment 1, two SBM samples (SBM1 and SBM2) from 2 different sources were subjected to porcine in vitro gastric degradation to determine the effects of protease (at 15,000 units/kg) on degradation of the soybean allergenic proteins. In Experiment 2, forty-eight weaned pigs (BW = 6.66 kg) were obtained in 2 batches of 24 pigs each. Pigs were individually housed in metabolic crates and fed 4 diets (12 pigs/diet). The diets were corn-based diet with SBM1 or SBM2 without or with protease at 15,000 units/kg in 2 × 2 factorial arrangement. Diets were fed for 10 days at the end of which the pigs were sacrificed for measurement of small intestinal histomorphology, permeability of small intestine mounted in Ussing chambers, and serum concentration of pro-inflammatory cytokines. The SBM1 and SBM2 contained 46.9 and 47.7% CP, 14.0 and 14.6% glycinin, and 9.90 and 10.3% β-conglycinin, respectively. Protease and SBM source did not interact on any of the response criteria measured in this study. Protease supplementation tended to increase (P = 0.069) the in vitro gastric degradation of glycinin by 20%. Protease supplementation tended to reduce (P = 0.099) fluorescein isothiocyanate dextran 4,000 Da (which is a marker probe for intestinal permeability) flow in jejunum by 33%, and reduced (P = 0.037) serum TNF-α concentration by 16%. Protease did not affect small intestinal histomorphology. In conclusion, protease increased gastric degradation of glycinin, and reduced gut permeability and serum concentration of pro-inflammatory cytokine, indicating that the protease used in the current study can be added in diets for weaned pigs to improve gut health of weaned pigs fed SBM-based diets.
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