메뉴 건너뛰기




Volumn 42, Issue C, 2004, Pages 407-414

Functional fish protein isolates prepared using low ionic strength, acid solubilization /precipitation

Author keywords

[No Author keywords available]

Indexed keywords


EID: 77957032500     PISSN: 01674501     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0167-4501(04)80040-2     Document Type: Article
Times cited : (7)

References (18)
  • 1
    • 0001205219 scopus 로고
    • Functional properties of muscle proteins
    • Hudson, and B.J.F. (Ed), Elsevier Appl. Sci., London,UK
    • Morrissey P.A., Mulvihill D.M., and O'Neill E.M. Functional properties of muscle proteins. In: Hudson, and B.J.F. (Ed). Developments in Food Proteins (1987), Elsevier Appl. Sci., London,UK 195-255
    • (1987) Developments in Food Proteins , pp. 195-255
    • Morrissey, P.A.1    Mulvihill, D.M.2    O'Neill, E.M.3
  • 3
    • 0011916364 scopus 로고
    • The influence of pH on the protein net charge in the myofibrillar system
    • Hamm R. The influence of pH on the protein net charge in the myofibrillar system. Reciprocal Meat Conference Proceedings 47 (1994) 5-9
    • (1994) Reciprocal Meat Conference Proceedings , vol.47 , pp. 5-9
    • Hamm, R.1
  • 4
    • 0012165343 scopus 로고    scopus 로고
    • Process for isolating a protein composition from a muscle source and protein composition
    • U.S. Patent Number 6,005,073. Issued Dec. 21
    • Hultin, H.O. and Kelleher, S.D. (1999) Process for isolating a protein composition from a muscle source and protein composition. U.S. Patent Number 6,005,073. Issued Dec. 21.
    • (1999)
    • Hultin, H.O.1    Kelleher, S.D.2
  • 6
    • 84981407132 scopus 로고
    • Rheological and calorimetric investigations of starch-fish protein systems during thermal processing
    • Wu M.C., Hamann D.D., and Lanier T.C. Rheological and calorimetric investigations of starch-fish protein systems during thermal processing. J. Tex. Studies 16 (1985) 53-74
    • (1985) J. Tex. Studies , vol.16 , pp. 53-74
    • Wu, M.C.1    Hamann, D.D.2    Lanier, T.C.3
  • 7
    • 0030093876 scopus 로고    scopus 로고
    • A simple and rapid solvent extraction method for determining total lipids in fish tissue
    • Lee C.M., Trevino B., and Chaiyawat M. A simple and rapid solvent extraction method for determining total lipids in fish tissue. J. AOAC Intl. 79 (1996) 487-492
    • (1996) J. AOAC Intl. , vol.79 , pp. 487-492
    • Lee, C.M.1    Trevino, B.2    Chaiyawat, M.3
  • 8
    • 84981865736 scopus 로고
    • Evaluation of the biuret and dye-binding methods for protein determination in meats
    • Torten J., and Whitaker J.R. Evaluation of the biuret and dye-binding methods for protein determination in meats. J. Food Sci. 29 (1969) 168-174
    • (1969) J. Food Sci. , vol.29 , pp. 168-174
    • Torten, J.1    Whitaker, J.R.2
  • 9
    • 0022556023 scopus 로고
    • Determination of phosphorus in cereal lipids
    • Kovacs M.I.P. Determination of phosphorus in cereal lipids. Anal. Biochem. 154 (1986) 420-423
    • (1986) Anal. Biochem. , vol.154 , pp. 420-423
    • Kovacs, M.I.P.1
  • 10
    • 0003787803 scopus 로고
    • New Series Circular No. 51, Halifax Laboratory, Halifax, Nova Scotia, Canada
    • New Series Circular No. 51. Lemo D.W. An improved TBA test for rancidity (1975), Halifax Laboratory, Halifax, Nova Scotia, Canada
    • (1975) An improved TBA test for rancidity
    • Lemo, D.W.1
  • 11
    • 0000742888 scopus 로고    scopus 로고
    • Effect of washing with and without antioxidants on quality retention of mackerel fillets during refrigerated and frozen storage
    • Richards M.P., Kelleher S.D., and Hultin H.O. Effect of washing with and without antioxidants on quality retention of mackerel fillets during refrigerated and frozen storage. J. Agric. Food Chem. 46 (1998) 4363-4371
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 4363-4371
    • Richards, M.P.1    Kelleher, S.D.2    Hultin, H.O.3
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0031328830 scopus 로고    scopus 로고
    • New developments in manufacturing of surimi and surimi seafood
    • Park J.W., Lin T.M., and Yongsawatdigul J. New developments in manufacturing of surimi and surimi seafood. Food Rev. Int. 13 (1997) 577-610
    • (1997) Food Rev. Int. , vol.13 , pp. 577-610
    • Park, J.W.1    Lin, T.M.2    Yongsawatdigul, J.3
  • 14
    • 0031323516 scopus 로고    scopus 로고
    • Solubility of the proteins of mackerel light muscle at low ionic strength
    • Feng Y., and Hultin H.O. Solubility of the proteins of mackerel light muscle at low ionic strength. J. Food Biochem. 21 (1997) 479-496
    • (1997) J. Food Biochem. , vol.21 , pp. 479-496
    • Feng, Y.1    Hultin, H.O.2
  • 15
    • 84987349189 scopus 로고
    • Heat gelation properties and protein extractability of beef myofibrils
    • Samejima K., Egelandsdal B., and Fretheim K. Heat gelation properties and protein extractability of beef myofibrils. J. Food Sci. 50 (1985) 1540-1546
    • (1985) J. Food Sci. , vol.50 , pp. 1540-1546
    • Samejima, K.1    Egelandsdal, B.2    Fretheim, K.3
  • 16
    • 0029739750 scopus 로고    scopus 로고
    • Gelation of beef heart surimi as affected by antioxidants
    • Srinivasan S., and Xiong Y.L. Gelation of beef heart surimi as affected by antioxidants. J. Food Sci. 61 (1996) 707-711
    • (1996) J. Food Sci. , vol.61 , pp. 707-711
    • Srinivasan, S.1    Xiong, Y.L.2
  • 18
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O.B. Molten globule and protein folding. Adv. Protein Chem. 47 (1995) 83-229
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.