Pressure-temperature relationship in the rate of casein digestion by trypsin.

Hydrostatic pressures of 500 to 700 atmospheres have been shown to accelerate the observed rate of certain processes both in living cells, e.g. the light-emitting oxidation of luminous bacteria, and in crude enzyme preparations at temperatures higher than the normal optimum.’ The present study provides exploratory data concerning the activity of a crystallized enzyme preparation, trypsin, in relation to temperature and pressure, with casein as substrate.