메뉴 건너뛰기




Volumn 48, Issue 3, 2000, Pages 880-884

Effect of extrusion temperature on the solubility and molecular weight of lentil bean flour proteins containing low cysteine residues

Author keywords

Extrusion temperature; Lentil bean flour; Protein solubility

Indexed keywords

CYSTEINE; DISULFIDE; THIOL DERIVATIVE; VEGETABLE PROTEIN;

EID: 0034030844     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf990328f     Document Type: Article
Times cited : (12)

References (25)
  • 2
    • 0004202155 scopus 로고
    • Association of Official Analytical Chemists: Washington, DC
    • AOAC. Official Methods of Analysis, 15th ed.; Association of Official Analytical Chemists: Washington, DC, 1990.
    • (1990) Official Methods of Analysis, 15th Ed.
  • 4
    • 0009642331 scopus 로고
    • Gel electrophoresis under denaturing conditions
    • Bollag, D. M., Edelstein, S. J., Eds.; Wiley-Liss: New York
    • Bollag, D. M.; Edelstein, S. J. Gel electrophoresis under denaturing conditions. In Protein Methods; Bollag, D. M., Edelstein, S. J., Eds.; Wiley-Liss: New York, 1991; pp 95-123.
    • (1991) Protein Methods , pp. 95-123
    • Bollag, D.M.1    Edelstein, S.J.2
  • 5
    • 0009204554 scopus 로고
    • A possible mechanism for thermal texturization of soybean protein
    • Burgess, L. D.; Stanley, D. W. A possible mechanism for thermal texturization of soybean protein. Can. Inst. Food Sci. Technol. J. 1976, 9, 228-231.
    • (1976) Can. Inst. Food Sci. Technol. J. , vol.9 , pp. 228-231
    • Burgess, L.D.1    Stanley, D.W.2
  • 6
    • 0003081480 scopus 로고
    • Direct colormetric assay of free sulfhydryl groups and disulfide bonds in suspensions of solubilized and particulate cereal proteins
    • Chan, K.-Y.; Wasserman, B. P. Direct colormetric assay of free sulfhydryl groups and disulfide bonds in suspensions of solubilized and particulate cereal proteins. Cereal Chem. 1993, 70, 22-26.
    • (1993) Cereal Chem. , vol.70 , pp. 22-26
    • Chan, K.-Y.1    Wasserman, B.P.2
  • 7
    • 0002407188 scopus 로고
    • Hydrophobic interaction chromatography
    • Janson, J.-C., Rydén, L., Eds.; VCH Publishers: New York
    • Eriksson, K.-O. Hydrophobic interaction chromatography. In Protein Purification; Janson, J.-C., Rydén, L., Eds.; VCH Publishers: New York, 1989; pp 207-226.
    • (1989) Protein Purification , pp. 207-226
    • Eriksson, K.-O.1
  • 8
    • 84986846079 scopus 로고
    • Gel formation in acidified aqueous suspensions of cereal flours
    • Jennings, A. C. Gel formation in acidified aqueous suspensions of cereal flours. J. Sci. Food Agric. 1978, 29, 963-974.
    • (1978) J. Sci. Food Agric. , vol.29 , pp. 963-974
    • Jennings, A.C.1
  • 9
    • 0030498477 scopus 로고    scopus 로고
    • Effect of cysteine on free radical production and protein modification in extruded wheat flour
    • Koh, B. K.; Karwe, M. V.; Schaich, K. M. Effect of cysteine on free radical production and protein modification in extruded wheat flour. Cereal Chem. 1996, 73, 115-122.
    • (1996) Cereal Chem. , vol.73 , pp. 115-122
    • Koh, B.K.1    Karwe, M.V.2    Schaich, K.M.3
  • 10
    • 0345162896 scopus 로고
    • Wheat protein
    • Lǎsztity, R., Ed.; CRC Press: Boca Raton, FL
    • Lǎsztity, R. Wheat protein. In The Chemistry of Cereal Proteins; Lǎsztity, R., Ed.; CRC Press: Boca Raton, FL, 1984; pp 13-88.
    • (1984) The Chemistry of Cereal Proteins , pp. 13-88
    • Lǎsztity, R.1
  • 11
    • 0000031953 scopus 로고    scopus 로고
    • Effect of extrusion temperature on solubility and molecular weight distribution of wheat flour proteins
    • Li, M.; Lee, T.-C. Effect of extrusion temperature on solubility and molecular weight distribution of wheat flour proteins. J. Agric. Food Chem. 1996a, 44, 763-768.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 763-768
    • Li, M.1    Lee, T.-C.2
  • 12
    • 0001459934 scopus 로고    scopus 로고
    • Effect of cysteine on the functional properties and microstructures of wheat flour extrudates
    • Li, M.; Lee, T.-C. Effect of cysteine on the functional properties and microstructures of wheat flour extrudates. J. Agric. Food Chem. 1996b, 44, 1871-1880.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 1871-1880
    • Li, M.1    Lee, T.-C.2
  • 13
    • 0001571319 scopus 로고    scopus 로고
    • The relationship of the extrusion temperature and the solubility and disulfide bond distribution of wheat proteins
    • Li, M.; Lee, T.-C. The relationship of the extrusion temperature and the solubility and disulfide bond distribution of wheat proteins. J. Agric. Food Chem. 1997, 45, 2711-2714.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 2711-2714
    • Li, M.1    Lee, T.-C.2
  • 14
    • 0000991112 scopus 로고    scopus 로고
    • Effect of cysteine on the molecular weight distribution and the disulfide cross-link of wheat flour proteins in extrudates
    • Li, M.; Lee, T.-C. Effect of cysteine on the molecular weight distribution and the disulfide cross-link of wheat flour proteins in extrudates. J. Agric. Food Chem. 1998, 46, 846-853.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 846-853
    • Li, M.1    Lee, T.-C.2
  • 15
    • 0001501002 scopus 로고
    • Effect of extrusion cooking on the nutritional quality of plant proteins
    • Phillips, R. D., Finley, J. W., Eds.; Dekker: New York
    • Phillips, R. D. Effect of extrusion cooking on the nutritional quality of plant proteins. In Protein Quality and the Effects of Processing; Phillips, R. D., Finley, J. W., Eds.; Dekker: New York, 1989; pp 219-246.
    • (1989) Protein Quality and the Effects of Processing , pp. 219-246
    • Phillips, R.D.1
  • 16
    • 0002474144 scopus 로고
    • Proteins: General
    • Pomeranz, Y., Ed.; Academic Press: San Diego, CA
    • Pomeranz, Y. Proteins: general. In Functional Properties of Food Components; Pomeranz, Y., Ed.; Academic Press: San Diego, CA, 1991; pp 147-189.
    • (1991) Functional Properties of Food Components , pp. 147-189
    • Pomeranz, Y.1
  • 17
    • 0027324399 scopus 로고
    • Effect of phospholipid on protein structure and solubility in the extrusion of lung proteins
    • Pruděncio-Ferreira, S. H.; Arěas, J. A. G. Effect of phospholipid on protein structure and solubility in the extrusion of lung proteins. Food Chem. 1993, 47, 111-119.
    • (1993) Food Chem. , vol.47 , pp. 111-119
    • Pruděncio-Ferreira, S.H.1    Arěas, J.A.G.2
  • 18
    • 0030507415 scopus 로고    scopus 로고
    • Formation of flavors during extrusion cooking
    • Riha, W., III; Ho, C.-T. Formation of flavors during extrusion cooking. Food Rev. Int. 1996, 12, 351-373.
    • (1996) Food Rev. Int. , vol.12 , pp. 351-373
    • Riha W. III1    Ho, C.-T.2
  • 20
    • 0029344475 scopus 로고
    • The combined application of supercritical fluid and extrusion technology
    • Rizvi, S. S. H.; Mulvaney, S. J.; Sokhey, A. S. The combined application of supercritical fluid and extrusion technology. Trends Food Sci. Technol. 1995, 6, 232-240.
    • (1995) Trends Food Sci. Technol. , vol.6 , pp. 232-240
    • Rizvi, S.S.H.1    Mulvaney, S.J.2    Sokhey, A.S.3
  • 21
    • 0001483388 scopus 로고
    • Texture-structure relationships in textured soy protein. V. Influence of pH and protein acylation on extrusion texturization
    • Simonsky, R. W.; Stanley, D. W. Texture-structure relationships in textured soy protein. V. Influence of pH and protein acylation on extrusion texturization. Can. Inst. Food Sci. Technol. J. 1982, 15, 294-301.
    • (1982) Can. Inst. Food Sci. Technol. J. , vol.15 , pp. 294-301
    • Simonsky, R.W.1    Stanley, D.W.2
  • 22
    • 0002320592 scopus 로고
    • Chemical and structural determinants of texture of fabricated foods
    • Stanley, D. W. Chemical and structural determinants of texture of fabricated foods. Food Technol. 1986, 40, 65-68.
    • (1986) Food Technol. , vol.40 , pp. 65-68
    • Stanley, D.W.1
  • 23
    • 0000030832 scopus 로고
    • Protein reactions during extrusion cooking
    • Mercier, C., Linko, P., Harper, J. M., Eds.; American Association of Cereal Chemists: St. Paul, MN
    • Stanley, D. W. Protein reactions during extrusion cooking. In Extrusion Cooking; Mercier, C., Linko, P., Harper, J. M., Eds.; American Association of Cereal Chemists: St. Paul, MN, 1989; pp 321-341.
    • (1989) Extrusion Cooking , pp. 321-341
    • Stanley, D.W.1
  • 24
    • 0001363407 scopus 로고
    • Polymerization and mechanical degradation kinetics of gluten and glutenin at extruder melt-section temperatures and shear rates
    • Strecker, T. D.; Cavalieri, R. P.; Zollars, R. L.; Pomeranz, Y. Polymerization and mechanical degradation kinetics of gluten and glutenin at extruder melt-section temperatures and shear rates. J. Food Sci. 1995, 60, 532-537, 557.
    • (1995) J. Food Sci. , vol.60 , pp. 532-537
    • Strecker, T.D.1    Cavalieri, R.P.2    Zollars, R.L.3    Pomeranz, Y.4
  • 25
    • 0004756573 scopus 로고
    • Changes in solubility and distribution of semolina proteins due to extrusion processing
    • Ummadi, P.; Chenoweth, W. L.; Ng, P. K. W. Changes in solubility and distribution of semolina proteins due to extrusion processing. Cereal Chem. 1995, 72, 564-567.
    • (1995) Cereal Chem. , vol.72 , pp. 564-567
    • Ummadi, P.1    Chenoweth, W.L.2    Ng, P.K.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.