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ABSTRACT

Various proteins were subjected to thermolysin digestion at 2000 atm. Casein and soy protein were extensively digested at both atmospheric and high pressures, but the tetrameric proteins alcohol dehydrogenase and hemoglobin and the monomeric protein β-lactoglobulin were degraded only upon pressurization. Globular proteins with many disulfide bonds (RNase A, lysozyme, and α-lactalbumin) resisted the proteolysis at both pressures. These observations led to the preferential digestion of β-lactoglobulin in cow's milk whey, thus simulating human milk protein. The versatility of pressure-induced proteolysis in food processing is also proposed.