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Volumn , Issue , 2017, Pages 473-502

High-pressure effects on proteins

Author keywords

[No Author keywords available]

Indexed keywords

EFFECT OF PRESSURE; EGG YOLKS; LOW TEMPERATURES; LOWER PRESSURES; PRESSURE TREATMENTS;

EID: 85052714074     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9780203755617     Document Type: Chapter
Times cited : (42)

References (62)
  • 1
    • 0001435569 scopus 로고
    • The coagulation of albumin by pressure
    • P. W. Bridgman, The coagulation of albumin by pressure. J. Biol. Chem.79:511 (1914).
    • (1914) J. Biol. Chem , vol.79 , pp. 511
    • Bridgman, P.W.1
  • 2
    • 0000637201 scopus 로고
    • Application of high pressure to food processing: Pressurization of egg white and yolk, and properties of gels formed
    • R. Hayashi, Y. Kawamura, T. Nakasa, and O. Okinaka, Application of high pressure to food processing: pressurization of egg white and yolk, and properties of gels formed, Agric. Biol Chem. 53:2935 (1989).
    • (1989) Agric. Biol Chem , vol.53 , pp. 2935
    • Hayashi, R.1    Kawamura, Y.2    Nakasa, T.3    Okinaka, O.4
  • 3
    • 0002862399 scopus 로고
    • Studies on the kinetics of protein dénaturation under high pressure
    • K. Suzuki, Studies on the kinetics of protein dénaturation under high pressure, Rev. Phys. Chem. Japan 29:91 (1960).
    • (1960) Rev. Phys. Chem. Japan , vol.29 , pp. 91
    • Suzuki, K.1
  • 4
    • 0015236387 scopus 로고
    • Reversible pressure-temperature dénaturation of chymotrypsinogen
    • S. A. Hawley, Reversible pressure-temperature dénaturation of chymotrypsinogen, Biochemistry70:2436 (1971).
    • (1971) Biochemistry , vol.70 , pp. 2436
    • Hawley, S.A.1
  • 5
    • 0015820466 scopus 로고
    • Pressure dénaturation of metmyoglobin
    • A. Zipp and W. Kauzmann, Pressure dénaturation of metmyoglobin, Biochemistry72:4217 (1973).
    • (1973) Biochemistry , vol.72 , pp. 4217
    • Zipp, A.1    Kauzmann, W.2
  • 9
    • 0028220701 scopus 로고
    • Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes
    • M. Gross and R. Jaenicke, Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes, Eur. J. Biochem. 221: 617 (1994).
    • (1994) Eur. J. Biochem , vol.221 , pp. 617
    • Gross, M.1    Jaenicke, R.2
  • 10
    • 0028650679 scopus 로고
    • Exploiting the effects of high hydrostatic pressure in biotechnological applications
    • V. V. Mozahev, K. Heremans, J. Frank, P. Masson, and C. Balny, Exploiting the effects of high hydrostatic pressure in biotechnological applications, Trends Biotechnol. 12:493(1994).
    • (1994) Trends Biotechnol , vol.12 , pp. 493
    • Mozahev, V.V.1    Heremans, K.2    Frank, J.3    Masson, P.4    Balny, C.5
  • 11
    • 0003028964 scopus 로고
    • Biological effects of high hydrostatic pressure on food micro-organisms
    • D. G. Hoover, C. Metrick, A. M. Papineau, D. F. Farkas, and D. Knorr, Biological effects of high hydrostatic pressure on food micro-organisms, Food Technol. 43:99(1989).
    • (1989) Food Technol , vol.43 , pp. 99
    • Hoover, D.G.1    Metrick, C.2    Papineau, A.M.3    Farkas, D.F.4    Knorr, D.5
  • 13
    • 0020017199 scopus 로고
    • High pressure effects on proteins and other biomolecules
    • K. Heremans, High pressure effects on proteins and other biomolecules, Ann. Rev. Biophys. Bioeng. 77:1 (1982).
    • (1982) Ann. Rev. Biophys. Bioeng , vol.77 , pp. 1
    • Heremans, K.1
  • 14
    • 0000376379 scopus 로고    scopus 로고
    • High pressure effects on the structure and phase behavior of model membrane systems
    • (J. L. Markley, C. Royer, and D. Northrup, eds.) Oxford University Press, New York
    • R. Winter, A. Landwehr, Th. Brauns, J. Erbes, C. Czeslik, and O. Reis, High pressure effects on the structure and phase behavior of model membrane systems, High Pressure Effects in Molecular Biophysics and Enzymology (J. L. Markley, C. Royer, and D. Northrup, eds.) Oxford University Press, New York, 1996, pp. 274-297.
    • (1996) High Pressure Effects in Molecular Biophysics and Enzymology , pp. 274-297
    • Winter, R.1    Landwehr, A.2    Brauns, T.H.3    Erbes, J.4    Czeslik, C.5    Reis, O.6
  • 15
    • 0019322409 scopus 로고
    • Pressure effect on the Arrhenius discontinuity in Ca2+-ATPase from sarcoplasmic reticulum. Evidence for lipid involvement
    • 2+-ATPase from sarcoplasmic reticulum. Evidence for lipid involvement, FEBS Lett.777:161 (1980).
    • (1980) FEBS Lett , vol.777 , pp. 161
    • Heremans, K.1    Wuytack, F.2
  • 16
    • 0029204505 scopus 로고
    • Pasteurization of food by hydrostatic pressure: Chemical aspects
    • B. Tauscher, Pasteurization of food by hydrostatic pressure: Chemical aspects, Z. Lebensm. Untersuch. -Forsch. 200:3 (1995).
    • (1995) Z. Lebensm. Untersuch. -Forsch , vol.200 , pp. 3
    • Tauscher, B.1
  • 17
    • 0000748473 scopus 로고
    • Pressure dependence of weak acid ionization in aqueous buffers
    • R. C. Neuman, Jr., W. Kauzmann, and A. Zipp, Pressure dependence of weak acid ionization in aqueous buffers, J. Phys. Chem.77:2687 (1973).
    • (1973) J. Phys. Chem , vol.77 , pp. 2687
    • Neuman, R.C.1    Kauzmann, W.2    Zipp, A.3
  • 18
    • 0000818472 scopus 로고
    • Reaction volume of protonic ionization for buffering agents. Prediction of pressure dependence of pH and pOH
    • Y. Kitamura and T. Itoh, Reaction volume of protonic ionization for buffering agents. Prediction of pressure dependence of pH and pOH, J. Sol. Chem.76:715 (1987).
    • (1987) J. Sol. Chem , vol.76 , pp. 715
    • Kitamura, Y.1    Itoh, T.2
  • 19
    • 0000065233 scopus 로고
    • The behaviour of proteins under pressure
    • (R. Winter and J. Jonas, eds), Kluwer Academic, Dordrecht
    • K. Heremans, The behaviour of proteins under pressure, High Pressure Chemistry, Biochemistry and Material Science(R. Winter and J. Jonas, eds), Kluwer Academic, Dordrecht, 1993, pp. 443-469.
    • (1993) High Pressure Chemistry, Biochemistry and Material Science , pp. 443-469
    • Heremans, K.1
  • 20
    • 0000421265 scopus 로고
    • Pressure tuning spectroscopy of the low-frequency Raman spectrum of liquid amides
    • K. Goossens, L. Smeller, and K. Heremans, Pressure tuning spectroscopy of the low-frequency Raman spectrum of liquid amides, J. Chem. Phys.99:5736 (1993).
    • (1993) J. Chem. Phys , vol.99 , pp. 5736
    • Goossens, K.1    Smeller, L.2    Heremans, K.3
  • 22
    • 0003108820 scopus 로고
    • Effect of hydrostatic pressure on starch gelatinisation, as determined by DTA
    • A. H. Muhr, R. E. Wetton, and J. M. V. Blanshard, Effect of hydrostatic pressure on starch gelatinisation, as determined by DTA, Carbohydr. Polym.2:91 (1982).
    • (1982) Carbohydr. Polym , vol.2 , pp. 91
    • Muhr, A.H.1    Wetton, R.E.2    Blanshard, J.M.V.3
  • 23
    • 0001862839 scopus 로고    scopus 로고
    • Pressure and temperature induced inactivation of microorganisms
    • (J. L. Mark-ley, C. Royer, and D. Northrup, eds.), Oxford University Press, New York
    • H. Ludwig, W. Scigalla, and B. Sojka, Pressure and temperature induced inactivation of microorganisms, High Pressure Effects in Molecular Biophysics and Enzymology (J. L. Mark-ley, C. Royer, and D. Northrup, eds.), Oxford University Press, New York, 1996, pp. 346-363.
    • (1996) High Pressure Effects in Molecular Biophysics and Enzymology , pp. 346-363
    • Ludwig, H.1    Scigalla, W.2    Sojka, B.3
  • 24
    • 0001411233 scopus 로고
    • The effect of pressure and temperature on the death rates of Lactobacillus casei and Escherichia coli
    • (C. Balny, R. Hayashi, K. Heremans, and P. Masson, eds.), John Libbey Eurotext Ltd, Montrouge
    • K. Sonoike, T. Setoyama, Y. Kuma, and S. Kobayashi, The effect of pressure and temperature on the death rates of Lactobacillus casei and Escherichia coli, High Pressure and Biotechnology (C. Balny, R. Hayashi, K. Heremans, and P. Masson, eds.), John Libbey Eurotext Ltd, Montrouge, 1992, pp. 297-302.
    • (1992) High Pressure and Biotechnology , pp. 297-302
    • Sonoike, K.1    Setoyama, T.2    Kuma, Y.3    Kobayashi, S.4
  • 25
    • 0028226052 scopus 로고
    • High pressure NMR spectroscopy of proteins and membranes
    • J. Jonas and A. Jonas, High pressure NMR spectroscopy of proteins and membranes, Annu. Rev. Biophys. Biomol. Struct.23:287 (1994).
    • (1994) Annu. Rev. Biophys. Biomol. Struct , vol.23 , pp. 287
    • Jonas, J.1    Jonas, A.2
  • 26
    • 0011232951 scopus 로고
    • Device for optical studies of fast reactions in solution as a function of pressure and temperature
    • (C. Balny, R. Hayashi, K. Heremans, and P. Masson, eds.), John Libbey Eurotext Ltd, Montrouge
    • J.-L. Saldana and C. Balny, Device for optical studies of fast reactions in solution as a function of pressure and temperature, High Pressure and Biotechnology (C. Balny, R. Hayashi, K. Heremans, and P. Masson, eds.), John Libbey Eurotext Ltd, Montrouge, 1992, pp. 529-531.
    • (1992) High Pressure and Biotechnology , pp. 529-531
    • Saldana, J.-L.1    Balny, C.2
  • 27
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • S. N. Timasheff, The control of protein stability and association by weak interactions with water: How do solvents affect these processes?, Annu. Rev. Biophys. Biomol. Struct. 22:67 (1993).
    • (1993) Annu. Rev. Biophys. Biomol. Struct , vol.22 , pp. 67
    • Timasheff, S.N.1
  • 28
    • 0000521535 scopus 로고
    • High pressure unfolding and aggregation of β-Lactoglobulin and the baroprotective effects of sucrose
    • E. M. Dumay, M. T. Kalichevsky, and J. C. Cheftel, High pressure unfolding and aggregation of β-Lactoglobulin and the baroprotective effects of sucrose, J. Agric. Food Chem.42:1861 (1994).
    • (1994) J. Agric. Food Chem , vol.42 , pp. 1861
    • Dumay, E.M.1    Kalichevsky, M.T.2    Cheftel, J.C.3
  • 29
    • 0028071439 scopus 로고
    • Arc repressor will not denature under pressure in the absence of water
    • A. C. Oliveira., L. P. Gaspar, A. T. Da Poian, and J. L. Silva, Arc repressor will not denature under pressure in the absence of water, J. Mol. Biol240:184 (1994).
    • (1994) J. Mol. Biol , vol.240 , pp. 184
    • Oliveira, A.C.1    Gaspar, L.P.2    Da Poian, A.T.3    Silva, J.L.4
  • 30
    • 0001929731 scopus 로고    scopus 로고
    • Pressure tuning spectroscopy of proteins: FTIR studies in the diamond anvil cell
    • (J. L. Markley, C. Royer, and D. Northrup, eds.), Oxford University Press, New York
    • K. Heremans, K. Goossens, and L. Smeller, Pressure tuning spectroscopy of proteins: FTIR studies in the diamond anvil cell, High Pressure Effects in Molecular Biophysics and Enzy-mology(J. L. Markley, C. Royer, and D. Northrup, eds.), Oxford University Press, New York, 1996, pp. 44-61.
    • (1996) High Pressure Effects in Molecular Biophysics and Enzy-Mology , pp. 44-61
    • Heremans, K.1    Goossens, K.2    Smeller, L.3
  • 31
    • 0028986739 scopus 로고
    • High pressure stabilization of a-chymotrypsin entrapped in reversed micelles of Aerosol OT in octane against thermal inactivation
    • R. V. Rariy, N. Bec, J.-L. Saldana, S. N. Nametkin, V. V. Mozhaev, N. L. Klyachko, A. V. Levashov, and C. Balny, High pressure stabilization of a-chymotrypsin entrapped in reversed micelles of Aerosol OT in octane against thermal inactivation, FEBS Lett. 364:98 (1995).
    • (1995) FEBS Lett , vol.364 , pp. 98
    • Rariy, R.V.1    Bec, N.2    Saldana, J.-L.3    Nametkin, S.N.4    Mozhaev, V.V.5    Klyachko, N.L.6    Levashov, A.V.7    Balny, C.8
  • 32
    • 0029208356 scopus 로고
    • The determination of the secondary structure of proteins at high pressure
    • L. Smeller, K. Goossens, and K. Heremans, The determination of the secondary structure of proteins at high pressure, Vibrational Spectrosc. 8:199 (1995).
    • (1995) Vibrational Spectrosc , vol.8 , pp. 199
    • Smeller, L.1    Goossens, K.2    Heremans, K.3
  • 33
    • 0001649515 scopus 로고
    • Normal and malignant human colonic tissues investigated by pressure-tuning FT-IR spectroscopy
    • P. T. T. Wong, S. Lacelle, and H. M. Yadzi, Normal and malignant human colonic tissues investigated by pressure-tuning FT-IR spectroscopy, Appl. Spectrosc.47:1830 (1993).
    • (1993) Appl. Spectrosc , vol.47 , pp. 1830
    • Wong, P.T.T.1    Lacelle, S.2    Yadzi, H.M.3
  • 34
    • 0001535203 scopus 로고
    • High pressure effects on starch: Structural change and rétrogradation
    • (C. Balny, R. Hayashi, K. Heremans, and P. Masson, eds.), John Libbey Eurotext Ltd, Montrouge
    • S. Ezaki and R. Hayashi, High pressure effects on starch: structural change and rétrogradation, High Pressure and Biotechnology (C. Balny, R. Hayashi, K. Heremans, and P. Masson, eds.), John Libbey Eurotext Ltd, Montrouge, 1992, pp. 163-165.
    • (1992) High Pressure and Biotechnology , pp. 163-165
    • Ezaki, S.1    Hayashi, R.2
  • 35
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • M. Jackson and H. H. Mantsch, The use and misuse of FTIR spectroscopy in the determination of protein structure, Crit. Rev. Biochem. Mol. Biol. 30:95 (1995).
    • (1995) Crit. Rev. Biochem. Mol. Biol , vol.30 , pp. 95
    • Jackson, M.1    Mantsch, H.H.2
  • 36
    • 0001502863 scopus 로고
    • High pressure-induced gel formation of a whey protein and haemoglobin protein concentrate
    • J. Van Camp and A. Huyghebaert, High pressure-induced gel formation of a whey protein and haemoglobin protein concentrate, Lebensm. Wiss. Technol.28:111 (1995).
    • (1995) Lebensm. Wiss. Technol , vol.28 , pp. 111
    • Van Camp, J.1    Huyghebaert, A.2
  • 37
    • 84987322003 scopus 로고
    • Dénaturation of bovine serum albumin (BSA) and ovalbumin by high pressure, heat and chemicals
    • I. Hayakawa, J. Kajihara, K. Morikawa, M. Oda, and Y. Fujio, Dénaturation of bovine serum albumin (BSA) and ovalbumin by high pressure, heat and chemicals, J. Food Sci. 57:288(1992).
    • (1992) J. Food Sci , vol.57 , pp. 288
    • Hayakawa, I.1    Kajihara, J.2    Morikawa, K.3    Oda, M.4    Fujio, Y.5
  • 39
    • 0000940306 scopus 로고
    • Pressure-induced aggregation of a f3-lactoglobulin isolate in different pH 7.0 buffers
    • S. Funtenberger, E. Dumay, and J. C. Cheftel, Pressure-induced aggregation of a f3-lactoglobulin isolate in different pH 7.0 buffers, Lebensm. Wiss. u Technol.28:410 (1995).
    • (1995) Lebensm. Wiss. U Technol , vol.28 , pp. 410
    • Funtenberger, S.1    Dumay, E.2    Cheftel, J.C.3
  • 40
    • 21144469137 scopus 로고
    • Production of low antigenic whey protein hydrolysates by enzymatic hydrolysis and dénaturation with high pressure
    • T. Nakamura, H. Sado, and Y. Syukunobe, Production of low antigenic whey protein hydrolysates by enzymatic hydrolysis and dénaturation with high pressure, Milchwissenschaft48:141 (1993).
    • (1993) Milchwissenschaft , vol.48 , pp. 141
    • Nakamura, T.1    Sado, H.2    Syukunobe, Y.3
  • 41
    • 0013587164 scopus 로고
    • Pressure effect on microorganisms and immunoglobulins of bovine colostrum
    • (C. Balny, R. Hayashi, K. Heremans, and P. Masson, eds.), John Libbey Eurotext Ltd, Montrouge
    • C. Tonello, A. Largeteau, F. Jolibert, A. Deschamps, and G. Demazeau. Pressure effect on microorganisms and immunoglobulins of bovine colostrum, High Pressure and Biotechnology (C. Balny, R. Hayashi, K. Heremans, and P. Masson, eds.), John Libbey Eurotext Ltd, Montrouge, 1992, pp. 249-253.
    • (1992) High Pressure and Biotechnology , pp. 249-253
    • Tonello, C.1    Largeteau, A.2    Jolibert, F.3    Deschamps, A.4    Demazeau, G.5
  • 42
    • 85127978335 scopus 로고
    • The basics of solid foods rheology
    • P. Moskowitz, edMarcel Dekker, New York
    • M. Peleg, The basics of solid foods rheology, Food Texture (P. Moskowitz, ed.), Marcel Dekker, New York, 1987, pp. 3-33.
    • (1987) Food Texture , pp. 3-33
    • Peleg, M.1
  • 44
    • 84998340844 scopus 로고
    • Properties of pressure-induced gels of various soy protein products
    • T. Matsumoto and R. Hayashi, Properties of pressure-induced gels of various soy protein products, Nipp. Nogei. Kaishi. 64:1455 (1990).
    • (1990) Nipp. Nogei. Kaishi , vol.64 , pp. 1455
    • Matsumoto, T.1    Hayashi, R.2
  • 45
    • 84872885475 scopus 로고
    • Application of high pressure to food processing: Textural comparison of pressure- and heat-induced gels of food proteins
    • M. Okamoto, Y. Kawamura, and R. Hayashi, Application of high pressure to food processing: textural comparison of pressure- and heat-induced gels of food proteins, Agric. Biol. Chem. 54:183 (1990).
    • (1990) Agric. Biol. Chem , vol.54 , pp. 183
    • Okamoto, M.1    Kawamura, Y.2    Hayashi, R.3
  • 46
    • 21144463602 scopus 로고
    • Properties of acid set gels prepared from high pressure treated skim milk
    • D. E. Johnston, B. A. Austin, and R. J. Murphy, Properties of acid set gels prepared from high pressure treated skim milk, Milchwissenschaft 48:206 (1993).
    • (1993) Milchwissenschaft , vol.48 , pp. 206
    • Johnston, D.E.1    Austin, B.A.2    Murphy, R.J.3
  • 47
    • 0028793284 scopus 로고
    • A comparative rheological study between heat and high pressure-induced whey protein gels
    • J. Van Camp, and A. Huyghebaert. A comparative rheological study between heat and high pressure-induced whey protein gels, Food Chem54:357 (1995).
    • (1995) Food Chem , vol.54 , pp. 357
    • Van Camp, J.1    Huyghebaert, A.2
  • 48
    • 0000355713 scopus 로고    scopus 로고
    • Pressure- and heat-induced gelation of mixed /3-lactoglobulin/xanthan solutions
    • D. V. Zasypkin, E. Dumay, and J. C. Cheftel, Pressure- and heat-induced gelation of mixed /3-lactoglobulin/xanthan solutions, Food Hydrocolloids 10:203 (1996).
    • (1996) Food Hydrocolloids , vol.10 , pp. 203
    • Zasypkin, D.V.1    Dumay, E.2    Cheftel, J.C.3
  • 50
    • 0019536747 scopus 로고
    • Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels
    • A. H. Clark, D. H. P. Saunderson, and A. Suggett, Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels, Int. J. Peptide Protein Res. 17:353 (1981).
    • (1981) Int. J. Peptide Protein Res , vol.17 , pp. 353
    • Clark, A.H.1    Saunderson, D.H.P.2    Suggett, A.3
  • 51
    • 0023693897 scopus 로고
    • Structural and conformational changes og fi-lactoglobulin B: And infrared spectroscopic stuy of the effect of pH and temperature
    • H. L. Casal, U. Kohler, and H. H. Mantsch, Structural and conformational changes og fi-lactoglobulin B: And infrared spectroscopic stuy of the effect of pH and temperature, Biochim. Biophys. Acta957:11 (1988).
    • (1988) Biochim. Biophys. Acta , vol.957 , pp. 11
    • Casal, H.L.1    Kohler, U.2    Mantsch, H.H.3
  • 53
    • 0001057371 scopus 로고
    • Pressure effects on the Raman spectra of proteins: Pressure-induced changes in the conformation of lysozyme
    • K. Heremans and P. T. T. Wong, Pressure effects on the Raman spectra of proteins: pressure-induced changes in the conformation of lysozyme, Chem. Phys. Lett.7/8:101 (1985).
    • (1985) Chem. Phys. Lett , vol.7 , Issue.8 , pp. 101
    • Heremans, K.1    Wong, P.T.T.2
  • 54
    • 0023727267 scopus 로고
    • Pressure effect on protein secondary structure and deuterium exchange in chymotrypsinogen: A Fourier transform infrared spectroscopic study
    • P. T. T. Wong and K. Heremans, Pressure effect on protein secondary structure and deuterium exchange in chymotrypsinogen: A Fourier transform infrared spectroscopic study, Biochem. Biophys. Acta956:1 (1988).
    • (1988) Biochem. Biophys. Acta , vol.956 , pp. 1
    • Wong, P.T.T.1    Heremans, K.2
  • 55
    • 84987378217 scopus 로고
    • Introduction of high pressure to food processing: Preferential proteolysis of /3-Lactoglobulin in milk whey
    • R. Hayashi, Y. Kawamura, and S. Kunugi, Introduction of high pressure to food processing: preferential proteolysis of /3-Lactoglobulin in milk whey, J. Food Sci.52:1107 (1987).
    • (1987) J. Food Sci , vol.52 , pp. 1107
    • Hayashi, R.1    Kawamura, Y.2    Kunugi, S.3
  • 56
    • 0000571049 scopus 로고
    • Conformational change of casein micelles by high pressure treatment
    • (C. Balny, R. Hayashi, K. Heremans, and P. Masson, eds.), John Libbey Eurotext Ltd, Montrouge
    • Y. Shibauchi, H. Yamamoto, and Y. Sagara, Conformational change of casein micelles by high pressure treatment, High Pressure and Biotechnology (C. Balny, R. Hayashi, K. Heremans, and P. Masson, eds.), John Libbey Eurotext Ltd, Montrouge, 1992, pp. 239-242.
    • (1992) High Pressure and Biotechnology , pp. 239-242
    • Shibauchi, Y.1    Yamamoto, H.2    Sagara, Y.3
  • 57
    • 0000081168 scopus 로고
    • Hydrostatic pressure-induced aggregation of myosin molecules in 0.5 M KC1 at pH 6.0
    • (C. Balny, R. Hayashi, K. Heremans, and P. Masson, eds.), John Libbey Eurotext Ltd, Montrouge
    • K. Yamamoto, S. Hayashi, and T. Yasui, Hydrostatic pressure-induced aggregation of myosin molecules in 0.5 M KC1 at pH 6.0, High Pressure and Biotechnology (C. Balny, R. Hayashi, K. Heremans, and P. Masson, eds.), John Libbey Eurotext Ltd, Montrouge, 1992, pp. 229-233.
    • (1992) High Pressure and Biotechnology , pp. 229-233
    • Yamamoto, K.1    Hayashi, S.2    Yasui, T.3
  • 58
    • 84986450026 scopus 로고
    • Pressure-induced dimerization of metmyoglobin
    • A. B. Defaye and D. A. Ledward, Pressure-induced dimerization of metmyoglobin, J. Food Sci. 60:262 (1995).
    • (1995) J. Food Sci , vol.60 , pp. 262
    • Defaye, A.B.1    Ledward, D.A.2
  • 59
    • 0028868228 scopus 로고
    • Renaturation of metmyoglobin subjected to high isostatic pressure
    • A. B. Defaye, D. A. Ledward, D. B. MacDougall, and R. F. Tester, Renaturation of metmyoglobin subjected to high isostatic pressure, Food Chem.52:19 (1995).
    • (1995) Food Chem , vol.52 , pp. 19
    • Defaye, A.B.1    Ledward, D.A.2    Macdougall, D.B.3    Tester, R.F.4
  • 60
    • 0001846085 scopus 로고
    • Effect of high pressure on texture and ultrastructure of fish and chicken muscles and their gels
    • (C. Balny, R. Hayashi, K. Heremans, and P. Masson, eds.), John Libbey Eurotext Ltd, Montrouge
    • K. Yoshioka, Y. Kage, and H. Omura, Effect of high pressure on texture and ultrastructure of fish and chicken muscles and their gels, High Pressure and Biotechnology (C. Balny, R. Hayashi, K. Heremans, and P. Masson, eds.), John Libbey Eurotext Ltd, Montrouge, 1992, pp. 325-327.
    • (1992) High Pressure and Biotechnology , pp. 325-327
    • Yoshioka, K.1    Kage, Y.2    Omura, H.3
  • 62
    • 0002914044 scopus 로고
    • The effect of pressure on certain microorganisms encountered in preserving fruits and vegetables
    • B. H. Hite, N. J. Giddings, and C. E. Weakly, The effect of pressure on certain microorganisms encountered in preserving fruits and vegetables, West. Va. Univ. Agr. Expt. Sta. Bull. 146:1 (1914).
    • (1914) West. Va. Univ. Agr. Expt. Sta. Bull , vol.146 , pp. 1
    • Hite, B.H.1    Giddings, N.J.2    Weakly, C.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.