Summary
Parameters of thermal death were determined in 10 strains of yeast species whose maximum temperatures for growth (T max) ranged from 22 to 49°C. Arrhenius plots of the specific thermal death rates (k d) formed a positional sequence at the level of the experimental points that corrresponded in all but one case to the sequence of the respective T max values. Extrapolated k d values at higher or lower temperatures no longer formed this sequence.
The correlation of the temperature functions with T max could be characterized in terms of a new activation parameter, for which the name thermal death activation constant is introduced. It has the following form: T.D.A. \(constant = \frac{{\Delta {\rm H} \ne }}{{T_{\max + n} }}\) − ΔS≠ where ΔH≠ and ΔS≠ are respectively the apparent heat and entropy of activation of thermal death and n is the number of degrees above T max (expressed in °K) at which the T.D.A. constant exists.
Seven mesophilic yeasts had a T.D.A. constant between 72 and 79 calxmol-1 degree-1 at n values between 1 and 4°. This suggested that the destructive process that limits k d in these strains is of the same species as one that contributes to the establishment of T max. Two psychrophilic yeasts apparently had a similar T.D.A. constant but at a high n value (about 12.5°C) which suggested that in these strains T max is governed by a destructive process unrelated to the one that underlies thermal death. The strain of the nearly thermophilic Hansenula angusta (T max 49°C) did not fit in either group.
The significance of the T.D.A. constant is discussed and expressions for ΔH≠ and ΔS≠ in terms of bond activation parameters are proposed.
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References
Biltonen, R.: Reversible conformational isomerization of α-chymotrypsin and various derivatives. Thesis, University of Minnesota, U.S.A. 1965.
Brandts, J. F.: Heat effects on proteins and enzymes. In: Rose, A. H.: Thermobiology, pp. 25–72. London-New York: Academic Press 1967.
Christophersen, J.: Mikroorganismen. In: Precht, H., J. Christophersen u. H. Hensel. Temperature und Leben, S. 178–328. Berlin-Göttingen-Heidelberg: Springer 1955.
Eyring, H.: The activated complex and the absolute rate of chemical reactions. Chem. Rev. 17, 65–77 (1935).
—, and A. E. Stearn: The application of the theory of absolute reaction rates to proteins. Chem. Rev. 24, 253–270 (1939).
Farrell, J., and A. H. Rose: Temperature effects on micro-organisms. In: Rose, A. H.: Thermobiology, pp. 147–218. London-New York: Academic Press 1967a.
——: Temperature effects on microorganisms. Ann. Rev. Microbiol. 21, 101–120 (1967b).
Hinshelwood, C. N.: The chemical kinetics of the bacterial cell. Oxford: Clarendon Press 1946.
Ingraham, J. L.: Temperature relationships. In: Gunsalus, I. C., and R. Y. Stanier: The Bacteria, Vol. IV, pp. 265–298. New York-London: Academic Press 1962.
Johnson, F. H., H. Eyring, and M. J. Polissar: The kinetic basis of molecular biology. New York: John Wiley & Sons, Inc. 1954.
Mirsky, A. E., and L. Pauling: On the structure of native, denatured and coagulated proteins. Proc. nat. Acad. Sci. (Wash.) 22, 439–447 (1936).
Stearn, A. E.: Kinetics of biological reactions with special reference to enzyme processes. Advance Enzymol. 9, 25–74 (1949).
Woese, C.: Thermal inactivation of animal viruses. Ann. N. Y. Acad. Sci. 83, 741–751 (1960).
Wood, T. H.: Lethal effects of high and low temperatures on unicellular organisms. Advance Biol. Med. Phys. 4, 119–165 (1956).
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van Uden, N., Abranches, P. & Cabeça-Silva, C. Temperature functions of thermal death in yeasts and their relation to the maximum temperature for growth. Archiv. Mikrobiol. 61, 381–393 (1968). https://doi.org/10.1007/BF00409674
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DOI: https://doi.org/10.1007/BF00409674