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Both urease and trypsin inhibitors (TI) are heat-sensitive, i.e., their activity decreases with heat treatment during SBM processing. Urease test is simpler method and thus used commonly which also indicates TI activity, i.e., adequacy of heat treatment applied to SBM. Although both are correlated, many times it is not directly proportional and hence less reliable indicator of TI levels.
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Great question Kim! First, urease is an enzyme present in soybeans and other legumes that is not biochemically related to trypsin inhibitors. Furthermore, this urease enzyme has no negative effect on the digestion or utilization of nutrients. Urease is not an antinutritional factor. So, why do we measure urease activity in soybean meal?
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When soybean meal is being processed, heat deactivates both urease and trypsin inhibitors
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When urease activty level is high, it shows trypsin inhibitor(s) is also high, which shows that, sbm is undercooked. The lower levels of unease and trypsin inhibitor(s), shows sbm has been processed properly.
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In conclusion, the current study showed that TI increases the endogenous loss of AA and reduced the digestibility of minerals in broiler chickens.
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Applying a treatment of 2500 MHz for 30 minutes, Zhong et al. (2015) managed to inactivate a significant amount of the trypsin inhibitor.
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