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Volumn 63, Issue 1, 1998, Pages 92-95

Textural Properties of Pressure-Induced Gels of Food Proteins Obtained under Different Temperatures including Subzero

Author keywords

food protein; gelation; high pressure; subzero; textural prop erties

Indexed keywords


EID: 85174221226     PISSN: 00221147     EISSN: 17503841     Source Type: Journal    
DOI: 10.1111/j.1365-2621.1998.tb15683.x     Document Type: Article
Times cited : (44)

References (22)
  • 2
    • 0000358270 scopus 로고
    • Role of the thermal denaturation-aggregation relationship in determining the rheological properties of heat-induced networks for ovalbumin and vicilin
    • Arntfield, S.D., Murray, E.D., Ismond, M.A.H., and Bernatsky, A.M. 1989. Role of the thermal denaturation-aggregation relationship in determining the rheological properties of heat-induced networks for ovalbumin and vicilin. J. Food Sci. 54: 1624-1631.
    • (1989) J. Food Sci. , vol.54 , pp. 1624-1631
    • Arntfield, S.D.1    Murray, E.D.2    Ismond, M.A.H.3    Bernatsky, A.M.4
  • 3
    • 0000583890 scopus 로고
    • Effects of various anions on the rheological and gelling behavior of soy proteins: Thermody-namic observations
    • Babajimopoulos, M., Damodaran, S., Rizvi, S.S.H., and Kinsella, J.E. 1983. Effects of various anions on the rheological and gelling behavior of soy proteins: thermody-namic observations. J. Agric. Food Chem. 31: 1270-1275.
    • (1983) J. Agric. Food Chem. , vol.31 , pp. 1270-1275
    • Babajimopoulos, M.1    Damodaran, S.2    Rizvi, S.S.H.3    Kinsella, J.E.4
  • 5
    • 84987310021 scopus 로고
    • Comparison of cold-, acid-and salt-precipitated soy proteins
    • Bau, H.M., Poullain, B., Beaufrand, M.J., and Debry, G. 1978. Comparison of cold-, acid-and salt-precipitated soy proteins. J. Food Sci. 43: 106-111.
    • (1978) J. Food Sci. , vol.43 , pp. 106-111
    • Bau, H.M.1    Poullain, B.2    Beaufrand, M.J.3    Debry, G.4
  • 6
    • 0010322234 scopus 로고
    • Disulfide and sulfhydryl groups in glycinin
    • Draper, M. and Castimopoolas, N. 1978. Disulfide and sulfhydryl groups in glycinin. Cereal Chem. 55: 16-22.
    • (1978) Cereal Chem , vol.55 , pp. 16-22
    • Draper, M.1    Castimopoolas, N.2
  • 8
    • 84981849482 scopus 로고
    • The texturometer. A new instrument for objective texture measurement
    • Friedman, H.H., Whitney, J.E., and Szczesniak, A.S. 1963. The texturometer. A new instrument for objective texture measurement. J. Food Sci. 28: 390-396.
    • (1963) J. Food Sci. , vol.28 , pp. 390-396
    • Friedman, H.H.1    Whitney, J.E.2    Szczesniak, A.S.3
  • 9
    • 84987261115 scopus 로고
    • Separation of phospholipids from egg yolk and recovery of water-soluble protein
    • Hatta, H., Sim, J.S., and Nakai, S. 1988. Separation of phospholipids from egg yolk and recovery of water-soluble protein. J. Food Sci. 53: 425-427.
    • (1988) J. Food Sci. , vol.53 , pp. 425-427
    • Hatta, H.1    Sim, J.S.2    Nakai, S.3
  • 10
    • 0015236387 scopus 로고
    • Reversible pressure-temperature denaturation of chymotrypsinogen
    • Hawley, S.A. 1971. Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry 10: 2436-2442.
    • (1971) Biochemistry , vol.10 , pp. 2436-2442
    • Hawley, S.A.1
  • 11
    • 84987322003 scopus 로고
    • Denaturation of bovine serum albumin (BSA) and ovalbumin by high pressure, heat and chemicals
    • Hayakawa, I., Kajihara, J., Morikawa, K., Oda, M., and Fujio, Y. 1992. Denaturation of bovine serum albumin (BSA) and ovalbumin by high pressure, heat and chemicals. J. Food Sci. 57: 288-292.
    • (1992) J. Food Sci. , vol.57 , pp. 288-292
    • Hayakawa, I.1    Kajihara, J.2    Morikawa, K.3    Oda, M.4    Fujio, Y.5
  • 12
    • 0001410369 scopus 로고
    • Application of high pressure to food processing and preservation: Philosophy and development
    • W.E.L. Spiess and H. Schubert (Ed.),, Elsevier Applied Science, London
    • Hayashi, R. 1989. Application of high pressure to food processing and preservation: philosophy and development. In Engineering and Food, Vol. 2. W.E.L. Spiess and H. Schubert (Ed.), p. 815-826. Elsevier Applied Science, London.
    • (1989) Engineering and Food , vol.2 , pp. 815-826
    • Hayashi, R.1
  • 13
    • 0000565077 scopus 로고
    • The hydrogen ion dissociation curve of the crystalline albumin of hen’s egg
    • Kekwick, R.A. and Cannan, R.K. 1936. The hydrogen ion dissociation curve of the crystalline albumin of hen’s egg. Biochem. J. 30: 227-234.
    • (1936) Biochem. J. , vol.30 , pp. 227-234
    • Kekwick, R.A.1    Cannan, R.K.2
  • 14
    • 0000047880 scopus 로고
    • Effects of reduction with dithiothreitol on some molecular properties of soy glycinin
    • Kim, S.H. and Kinsella, J.E. 1986. Effects of reduction with dithiothreitol on some molecular properties of soy glycinin. J. Agric. Food Chem. 34: 623-627.
    • (1986) J. Agric. Food Chem. , vol.34 , pp. 623-627
    • Kim, S.H.1    Kinsella, J.E.2
  • 15
    • 84985209713 scopus 로고
    • Studies on freeze-thaw gelation of very low density lipoprotein from hen’s egg yolk
    • Kurisaki, J.I., Kaminogawa, S., and Yamauchi, K. 1980. Studies on freeze-thaw gelation of very low density lipoprotein from hen’s egg yolk. J. Food Sci. 45: 463-466.
    • (1980) J. Food Sci. , vol.45 , pp. 463-466
    • Kurisaki, J.I.1    Kaminogawa, S.2    Yamauchi, K.3
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0345341764 scopus 로고    scopus 로고
    • Gelation of surimi pastes treated by high isostatic pressure
    • R. Hayashi and C. Balny (Ed.), Elsevier Science BV, Amsterdam
    • Lanier, T.C. 1996. Gelation of surimi pastes treated by high isostatic pressure. In High Pressure Bioscience and Biotechnology. R. Hayashi and C. Balny (Ed.), p. 357-361. Elsevier Science BV, Amsterdam.
    • (1996) High Pressure Bioscience and Biotechnology , pp. 357-361
    • Lanier, T.C.1
  • 18
    • 0026907780 scopus 로고
    • Application of high pressure and thermophysical properties of water to biotechnology
    • Makita, T. 1992. Application of high pressure and thermophysical properties of water to biotechnology. Fluid Phase Equilibra 76: 87-95.
    • (1992) Fluid Phase Equilibra , vol.76 , pp. 87-95
    • Makita, T.1
  • 19
    • 84872885475 scopus 로고
    • Application of high pressure to food processing: Textural comparison of pressure-and heat-induced gels of food pro-teins
    • Okamoto, M., Kawamura, Y., and Hayashi, R. 1990. Application of high pressure to food processing: textural comparison of pressure-and heat-induced gels of food pro-teins. Agric. Biol. Chem. 54: 183-189.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 183-189
    • Okamoto, M.1    Kawamura, Y.2    Hayashi, R.3
  • 20
    • 50549180355 scopus 로고
    • The gelation of ovalbumin solutions by high pres-sures
    • Suzuki, K. and Suzuki, C. 1963. The gelation of ovalbumin solutions by high pres-sures. Arch. Biochem. Biophysic. 102: 367-372.
    • (1963) Arch. Biochem. Biophysic. , vol.102 , pp. 367-372
    • Suzuki, K.1    Suzuki, C.2
  • 21
    • 33947094131 scopus 로고
    • Major proteins of soybean seeds. Subunits structure of -conglycinin
    • Thanh, V.H. and Shibasaki, K. 1978. Major proteins of soybean seeds. Subunits structure of -conglycinin. J. Agric. Food Chem. 26: 692-698.
    • (1978) J. Agric. Food Chem. , vol.26 , pp. 692-698
    • Thanh, V.H.1    Shibasaki, K.2
  • 22
    • 0030497201 scopus 로고    scopus 로고
    • High pressure-induced gel formation of haemoglobin and whey proteins at elevated temperatures
    • Van Camp, J., Feys, G., and Huyghebaert, A. 1996. High pressure-induced gel formation of haemoglobin and whey proteins at elevated temperatures. Lebens.-Wiss.u-Tech-nol. 29: 49-57.
    • (1996) Lebens.-Wiss.U-Tech-Nol. , vol.29 , pp. 49-57
    • van Camp, J.1    Feys, G.2    Huyghebaert, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.