The Effects of Pressure on Biopolymers and the Role of Water

Kunihiko Gekko

doi:10.4131/jshpreview.1.204

Kunihiko Gekko

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JOURNAL FREE ACCESS

1992 Volume 1 Issue 3 Pages 204-210

DOI https://doi.org/10.4131/jshpreview.1.204

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Published: August 20, 1992 Received: July 10, 1992 Available on J-STAGE: August 07, 2009 Accepted: - Advance online publication: - Revised: -
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Date of correction: August 07, 2009 Reason for correction: - Correction: CITATION Details: Wrong : [7] K. Gekko, H. Noguchi: J. Phys. Chem. , 83, 2706-2714 (1979), "Compressibility of globular proteins in water at 25°C. "
[8] K. Gekko, Y. Hasegawa: Biochemistry, 25, 6563-6571 (1986), “Compressibility-structure relationship of globular proteins. ”; J. Phys. Chem. , 93, 426-429 (1989), “Effect of temperature on the compressibility of native globular proteins. ”
[9] K. Gekko, K. Yamagami: J. Agric. Food Chem. , 39, 57-62 (1991), “Flexibility of food proteins as revealed by compressibility. ”
[10] E. Kundrot, F. M. Richards: J. Mol. Biol. , 193, 157-170 (1987), “Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres. ”
[11] H. Frauenfelder, H. Hartmann, M. Karplus, I. D. Kuntz, J. Kuriyan, F. Parak, G. A. Pet-sko, D. Ringe, R. F. Tilton, M. L. Connolly, N. Max: Biochemistry, 26, 254-261 (1987), “Thermal expansion of a protein. ”
[12] R. F. Tilton, Jr. , J. C. Dewan, G. A. Petsko: Biochemistry, 31, 2469-2481 (1992), “Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease A at nine different temperatures from 98 to 320K. ”
[13] R. Jaenicke: Ann. Rev. Biophys. Bioeng. , 10, 1-67 (1981), “Enzymes under extremes of physical conditions. ” ; Eur. J. Biochem. , 202, 715-728 (1991), “Protein stability and molecular adautation to extreme conditions. ”
[14] K. Heremans: Ann. Rev. Biophys. Bioeng. , 11, 1-21 (1982), “High pressure effects on pro teins and other biomolecules. ”
[15] K. Ohmiya, T. Kajino, S. Shimizu, K. Gekko: Agric. Biol. Chem. , 53, 1-7 (1989), “Effect of pressure on the association states of enzyme-treated caseins. ”
[16] K. Ruan, G. Weber: Biochemistry, 28, 2144-2153 (1989), “Hysteresis and conformational drift of pressure - dissociated glyceraldehyde-phosphate dehydrogenase. ”
[17] J. F. Brants, R. J. Oliveira, C. Westort: Bio-chemistry, 9, 1038-1047 (1970), “Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A. ”
[18] S. A. Hawley: Biochemistry, 10, 2436-2442 (1971), “Reversible pressure-temperature denaturation of chymotrypsnogen. ”
[19] A. Zipp, W. Kauzmann: Biochemistry, 12, 4217-4228 (1973), “Pressure denaturation of metmyoglobin. ”
[20] L. B∅je, A. Hvidt: Biopolymers, 11, 2357-2364 (1972), "Volume effects in aqueous solutions of macromolecules containing non-polar groups.
[22] K. Gekko, M. Fukamizu: Int. J. Biol. Macromol. , 13, 295-300 (1991), “Effect of pressure on the sol-gel transition of gelatin. ”
[23] K. Gekko, M. Fukamizu: Agric. Biol. Chem. , 55, 2427-2428 (1991), “Effect of pressure on the sol-gel transition of agarose. ”
[24] K. Gekko, K. Kasuya: Int. J. Biol. Macromol. , 7, 299-305 (1985), “Effect of pressure on the sol - gel transition of carrageenans. ”
[25] K. Ohmiya, K. Fukami, S. Shimizu, K. Gekko: J. Food. Sci. , 52, 84-87 (1987), “Milk curdling by rennet under high pressure. ”

Right : [7] K. Gekko, H. Noguchi: J. Phys. Chem. , 83, 2706-2714 (1979), “Compressibility of globular proteins in water at 25°C. ”
[8] K. Gekko, Y. Hasegawa: Biochemistry, 25, 6563-6571 (1986), “Compressibility-structure relationship of globular proteins. ”; J. Phys. Chem. , 93, 426-429 (1989), “Effect of temperature on the compressibility of native globular proteins. ”
[9] K. Gekko, K. Yamagami: J. Agric. Food Chem. , 39, 57-62 (1991), “Flexibility of food proteins as revealed by compressibility. ”
[10] E. Kundrot, F. M. Richards: J. Mol. Biol. , 193, 157-170 (1987), “Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres. ”
[11] H. Frauenfelder, H. Hartmann, M. Karplus, I. D. Kuntz, J. Kuriyan, F. Parak, G. A. Pet-sko, D. Ringe, R. F. Tilton, M. L. Connolly, N. Max: Biochemistry, 26, 254-261 (1987), “Thermal expansion of a protein. ”
[12] R. F. Tilton, Jr. , J. C. Dewan, G. A. Petsko: Biochemistry, 31, 2469-2481 (1992), “Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease A at nine different temperatures from 98 to 320K. ”
[13] R. Jaenicke: Ann. Rev. Biophys. Bioeng. , 10, 1-67 (1981), “Enzymes under extremes of physical conditions. ” ; Eur. J. Biochem. , 202, 715-728 (1991), “Protein stability and molecular adautation to extreme conditions. ”
[14] K. Heremans: Ann. Rev. Biophys. Bioeng. , 11, 1-21 (1982), “High pressure effects on pro teins and other biomolecules. ”
[15] K. Ohmiya, T. Kajino, S. Shimizu, K. Gekko: Agric. Biol. Chem. , 53, 1-7 (1989), “Effect of pressure on the association states of enzyme-treated caseins. ”
[16] K. Ruan, G. Weber: Biochemistry, 28, 2144-2153 (1989), “Hysteresis and conformational drift of pressure - dissociated glyceraldehyde-phosphate dehydrogenase. ”
[17] J. F. Brants, R. J. Oliveira, C. Westort: Bio-chemistry, 9, 1038-1047 (1970), “Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A. ”
[18] S. A. Hawley: Biochemistry, 10, 2436-2442 (1971), “Reversible pressure-temperature denaturation of chymotrypsnogen. ”
[19] A. Zipp, W. Kauzmann: Biochemistry, 12, 4217-4228 (1973), “Pressure denaturation of metmyoglobin. ”
[20] L. Bøje, A. Hvidt: Biopolymers, 11, 2357-2364 (1972), “Volume effects in aqueous solutions of macromolecules containing non-polar groups.”.
[22] K. Gekko, M. Fukamizu: Int. J. Biol. Macromol. , 13, 295-300 (1991), “Effect of pressure on the sol-gel transition of gelatin. ”
[23] K. Gekko, M. Fukamizu: Agric. Biol. Chem. , 55, 2427-2428 (1991), “Effect of pressure on the sol-gel transition of agarose. ”
[24] K. Gekko, K. Kasuya: Int. J. Biol. Macromol. , 7, 299-305 (1985), “Effect of pressure on the sol - gel transition of carrageenans. ”
[25] K. Ohmiya, K. Fukami, S. Shimizu, K. Gekko: J. Food. Sci. , 52, 84-87 (1987), “Milk curdling by rennet under high pressure. ”

Abstract

The application of high pressure technology to food processing and bioscience is a current topic. Water is the main component in such multicomponent systems to control their macroscopic properties and function. Under high pressure, water is not only the medium propagating pressure, but also it affects the stability and function of biopolymers through the modification of hydrogen bonds, hydrophobic and electrostatic interactions. This review is devoted to demonstrate how the biopolymer-water interaction (hydration) is related to the pressure effects on its structural stability, focusing on the compressibility, pressure denaturation, and gelation of proteins.

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