Glass transition explanation for the effect of polyhydroxy compounds on protein denaturation in dehydrated solids

Journal of Food Science

Volumn 61, Issue 2, 1996, Pages 372-375

  Bell, Leonard N ^a   Hageman, Michael J ^b  

^a AUBURN UNIVERSITY   (United States)

^b PFIZER INC   (United States)

Author keywords

Denaturation; Dry solids; Glass transition; Polyhydroxy; Protein

Indexed keywords

EID: 0000664156     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.1996.tb14196.x     Document Type: Article

References (30)

1. Arntfield, S.D., Murray, E.D., and Ismond, M.A.H. 1985. The influence of processing parameters on food protein functionality III. effect of moisture content on the thermal stability of fababean protein. Can. Inst. Food Sci. Technol. J. 18: 226-232.
2. Bell, L.N., Hageman, M.J., and Bauer, J.M. 1995a. Impact of moisture on thermally induced denaturation and decomposition of lyophilized bovine somatotropin. Biopolymers 35: 201-209.
3. Bell, L.N., Hageman, M.J., and Muraoka, L.M. 1995b. Thermally-induced denaturation of lyophilized bovine somatotropin and lysozyme as impacted by moisture and excipients. J. Pharm. Sci. 84: 707-712.
4. Fan, J., Cooper, E.I., and Angell, C.A. 1994. Glasses with strong calorimetric β-glass transitions and the relation to the protein glass transition problem. J. Phys. Chem. 98: 9345-9349.
5. Franks, F., Hatley, R.H.M., and Mathias, S.F. 1991. Materials science and the production of shelf-stable biologicals. BioPharm. 4(9): 38-42, 55.
6. Fujita, Y. and Noda, Y. 1978. Effect of hydration on the thermal denaturation of lysozyme as measured by differential scanning calorimetry. Bull. Chem. Soc. Jpn. 51: 1567-1568.
7. Fujita, Y. and Noda, Y. 1981a. The effect of hydration on the thermal stability of ovalbumin as measured by means of differential scanning calorimetry. Bull. Chem. Soc. Jpn. 54: 3233-3234.
8. Fujita, Y. and Noda, Y. 1981b. Effect of hydration on the thermal stability of protein as measured by differential scanning calorimetry: chymotrypsinogen. Int. J. Peptide Protein Res. 18: 12-17.
9. Green, J.L., Fan, J., and Angell, C.A. 1994. The protein-glass analogy: some insights from homopeptide comparisons. J. Phys. Chem. 98: 13780-13790.
10. Hageman, M.J. 1992. Water sorption and solid-state stability of proteins. Ch. 10 in Stability of Protein Pharmaceuticals, Part A: Chemical and Physical Pathways of Protein Degradation, T.J. Ahern and M.C. Manning (Ed.), p. 273-309. Plenum Press, New York.
11. Hagerdal, B. and Martens, H. 1976. Influence of water content on the stability of myoglobin to heat treatment. J. Food Sci. 41: 933-937.
12. Hoseney, R.C., Zeleznak, K., and Lai, C.S. 1986. Wheat gluten: a glassy polymer. Cereal Chem. 63: 285-286.
13. Kalichevsky, M.T., Blanshard, J.M.V., and Tokarczuk, P.F. 1993. Effect of water content and sugars on the glass transition of casein and sodium caseinate. Int. J. Food Sci. Technol. 28: 139-151.
14. Kalichevsky, M.T., Jaroszkiewicz, E.M., and Blanshard, J.M.V. 1992. Glass transition of gluten. 1: gluten and gluten-sugar mixtures. Int. J. Biol. Macromol. 14: 257-266.
15. Luescher, M., Ruegg, M., and Schindler, P. 1974. Effect of hydration upon the thermal stability of tropocollagen and its dependence on the presence of neutral salts. Biopolymers 13: 2489-2503.
16. Pikal, M.J. 1992, Freeze Drying in Encyclopedia of Pharmaceutical Technology, Vol. 6, J. Swarbrick and J.C. Boylan (Ed.), p. 275-303. Marcel Dekker, New York.
17. Roos, Y. and Karel, M. 1990. Differential scanning calorimetry study of phase transitions affecting the quality of dehydrated materials. Biotechnol. Prog. 6: 159-163.
18. Roy, M.L., Pikal, M.J., Rickard, B.C., and Maloney, A.M. 1992. The effects of formulation and moisture on the stability of a freeze-dried monoclonal antibody-vinca conjugate: a test of the WLF glass transition theory. Develop. Biol. Standard 74: 323-340.
19. Ruegg, M., Moor, U., and Blanc, B. 1975. Hydration and thermal denaturation of β-lactoglobulin: a calorimetric study. Biochim. Biophys. Acta 400: 334-342.
20. Saleki-Gerhardt, A. and Zografi, G. 1994. Non-isothermal and isothermal crystallization of sucrose from the amorphous state. Pharm. Res. 11: 1166-1173.
21. Sessa, D.J. 1992. Hydration effects on the thermal stability of proteins in cracked soybeans and defatted soy flour. Lebensm. Wiss. u. Technol. 25: 365-370.
22. Sheard, P.R., Fellows, A., Ledward, D.A., and Mitchell, J.R. 1986. Macromolecular changes associated with the heat treatment of soya isolate. J. Food Technol. 21: 55-60.
23. Slade, L. and Levine, H. 1988. Non-equilibrium behavior of small carbohydrate-water systems. Pure Appl. Chem. 60: 1841-1864.
24. Slade, L. and Levine, H. 1995. Glass transitions and water-food structure interactions, in Advances in Food and Nutrition Research, Vol. 38, S.L. Taylor and J.E. Kinsella (Ed.), p. 103-269. Academic Press, San Diego.
25. Slade, L., Levine, H., and Finley, J.W. 1989. Protein-water interactions: water as a plasticizer of gluten and other protein polymers. Ch. 2 in Protein Quality and the Effects of Processing, R.D. Phillips and J.W. Finley, (Ed.), p. 9-124. Marcel Dekker, New York.
26. Sochava, I.V. and Smirnova, O.I. 1993. Heat capacity of hydrated and dehydrated globular proteins - denaturation increment of heat capacity. Food Hydrocolloids 6: 513-524.
27. Sperling, L.H. 1986. Introduction to Physical Polymer Science, p. 224-295. John Wiley & Sons, New York.
28. Stanley, D.W. and Yada, R.Y. 1992. Physical consequences of thermal reactions in food protein systems. Ch. 16 in Physical Chemistry of Foods, H.G. Schwartzberg and R.W. Hartel (Ed.), p. 669-733. Marcel Dekker, New York.
29. Wagner, G. and Wüthrich, K. 1979. Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor. J. Mol. Biol. 130: 31-37.
30. Weast, R.C. (Ed.). 1972. Handbook of Chemistry and Physics, 53rd ed. The Chemical Rubber Company., Cleveland, OH.