Abstract
The effects of chemical modification of amino groups on the conformational stability of Mucor miehei proteinase (MMP), porcine pepsin, and chymosin, the latter two being from mammalian sources, were examined using kinetic and thermodynamic analyses. Modification-induced stability reduction of only MMP was observed as demonstrated by a higher rate of guanidine hydrochloride-induced denaturation, lower activation energy, decreased enthalpy of denaturation, and a substantially reduced free energy of denaturation. Results from this study corroborate those of a companion investigation [J. L. Smith et al., Agric. Biol. Chem., 55, 2009 (1991)] indicating that MMP was more susceptible to destabilization by charge alteration than aspartyl proteinases of mammalian origin.
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