The Canadian government has recently passed a law that will ban certain cattle tissues from all animal feeds, pet foods, and fertilizers. While established outlets for MBM are threatened, the supply of MBM is tied to meat production and thus relatively unresponsive to changes in demand. The development of alternative outlets for MBM is impeded by a couple of important barriers. Most proposed applications for MBM, other than as a fuel, would take advantage of the functional properties of MBM protein. These functional properties are inaccessible unless the highly degraded MBM protein is somehow made soluble, usually by hydrolysis. An application that successfully harnesses the protein��s functional properties could be rejected due to concerns of BSE prion Benzoylpaeoniflorin contamination. BSE prions are relatively resistant to hydrolysis, compared to other proteins. Prion-contaminated tissue can be rendered noninfective by extended alkaline hydrolysis, but the resulting material is extremely degraded and salty and retains little value. Several research groups have identified enzymes capable of digesting prion proteins, while other groups have developed methods to increase the prion��s susceptibility to protease digestion. However, all past demonstrations have presented the prions to the proteases in a ��best case�� scenario; typically raw, homogenized neural tissue diluted with buffer is treaded with the enzyme. These scenarios ignore the mass transport Acetrizoic acid barriers the MBM could impose, limiting access of enzyme to prions distributed within MBM particles. Hypothetically, prions could be protected from enzymatic attack by the matrix of rendered soft tissue or bone in which they would exist. The enzyme may not be able to diffuse into fat-laden particles or calcified bone tissue. Further, the overall rate of proteolytic MBM digestion depends greatly on whether the protease can penetrate deep within individual particles, or if the protease can only act near the surface of the particle. Enzymatic digestion from the surface only might be too slow for practical use. The present research uses the commercial protease VersazymeTM, and treats its ability to inactivate BSE prions as a given, based on previous literature.