Abstract

Thermal denaturation of four Carica papaya cysteine proteinases (papain, chymopapain, papaya proteinases 3 and 4) was studied as a function of pH using high-sensitivity differential scanning calorimetry. The ratios of calorimetric enthalpy to Van't Hoff enthalpy suggest that, for all these proteins, denaturation occurs as a non two state process, via an intermediate structure. Differences in the thermal stabilities of the proteinases; chymopapain > papaya proteinase 3 > papain > papaya proteinase 4, were correlated to their amino acid sequence to explain the observations in terms of mobility and specific residue mutation. Three-dimensional structures of papain and papaya proteinase 3 were similarly used to illustrate the influence of atomic mobility on stability. Study holds ProTherm entries: 7577, 7578, 7579, 7580, 7581, 7582, 7583, 7584, 7585, 7586, 7587, 7588, 7589, 7590, 7591, 7592, 7593, 7594, 7595, 7596 Extra Details:

Submission Details

ID: MWVJ5Cea3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:34 p.m.

Version: 1

Publication Details

Sumner IG;Harris GW;Taylor MA;Pickersgill RW;Owen AJ;Goodenough PW,Eur. J. Biochem. (1993) Factors effecting the thermostability of cysteine proteinases from Carica papaya. PMID:8508784

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