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Volumn 68, Issue 1, 2003, Pages 164-167

Optimum time for using chilled beef in gelled products

Author keywords

Beef; Free amino acids; Gelation; Malondialdehyde; Torsion test

Indexed keywords


EID: 0037283798     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2003.tb14134.x     Document Type: Article
Times cited : (15)

References (27)
  • 1
    • 0003995078 scopus 로고
    • Washington, D.C.: Association of Official Analytical Chemists
    • [AOAC] Association of Official Analytical Chemists. 1990. Official methods of analysis, 15th ed. Washington, D.C.: Association of Official Analytical Chemists.
    • (1990) Official Methods of Analysis, 15th Ed.
  • 2
    • 0001688999 scopus 로고    scopus 로고
    • Measurement of Malondialdehyde levels in food by high-performance liquid chromatography with fluorometric detection
    • Bergamo P, Fedele E, Bulestreieri M, Abrescia P, Ferrara L. 1998. Measurement of Malondialdehyde levels in food by high-performance liquid chromatography with fluorometric detection. J Agric Food Chem 46:2171-6.
    • (1998) J Agric Food Chem , vol.46 , pp. 2171-2176
    • Bergamo, P.1    Fedele, E.2    Bulestreieri, M.3    Abrescia, P.4    Ferrara, L.5
  • 3
    • 0013340670 scopus 로고    scopus 로고
    • Changes in pH and free amino acids in sheepmeat during extended chilled storage
    • Yokohama, Japan. Tokyo, Japan: Japan Society for Meat Science and Technology
    • Braggins TJ, Frost DA, Agnew MP, Podmore C. 1999. Changes in pH and free amino acids in sheepmeat during extended chilled storage. Proc. 45th ICoMST. Yokohama, Japan. Vol II. Tokyo, Japan: Japan Society for Meat Science and Technology. p 416-7.
    • (1999) Proc. 45th ICoMST , vol.2 , pp. 416-417
    • Braggins, T.J.1    Frost, D.A.2    Agnew, M.P.3    Podmore, C.4
  • 4
    • 84986430573 scopus 로고
    • Accelerated denaturation of myosin in frozen solution
    • Butkus H. 1970. Accelerated denaturation of myosin in frozen solution. J Food Sci 35:558-62.
    • (1970) J Food Sci , vol.35 , pp. 558-562
    • Butkus, H.1
  • 5
    • 0035490734 scopus 로고    scopus 로고
    • Role of pH in gel formation of washed chicken muscle at low ionic strength
    • Chang H, Feng Y, Hultin HO. 2001. Role of pH in gel formation of washed chicken muscle at low ionic strength. J Food Biochem 25:439-57.
    • (2001) J Food Biochem , vol.25 , pp. 439-457
    • Chang, H.1    Feng, Y.2    Hultin, H.O.3
  • 6
    • 50549155240 scopus 로고
    • The effect of carnosine and anserine on glycolytic reactions in skeletal muscle
    • Davey CL. 1960. The effect of carnosine and anserine on glycolytic reactions in skeletal muscle. Arch Biochem Biophy 89:296-302.
    • (1960) Arch Biochem Biophy , vol.89 , pp. 296-302
    • Davey, C.L.1
  • 7
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonal-dehyde and related aldehydes
    • Esterbauer, H, Schaur RJ, Zollner H. 1991. Chemistry and biochemistry of 4-hydroxynonenal, malonal-dehyde and related aldehydes. Free Rad Biol Meal 11:81-128.
    • (1991) Free Rad Biol Meal , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 8
    • 0031286044 scopus 로고    scopus 로고
    • Effect of pH at time of salting on the functional properties of pre-rigor beef
    • Farouk MM, Swan JE. 1997. Effect of pH at time of salting on the functional properties of pre-rigor beef. Meat Sci 45:463-472.
    • (1997) Meat Sci , vol.45 , pp. 463-472
    • Farouk, M.M.1    Swan, J.E.2
  • 9
    • 0032219597 scopus 로고    scopus 로고
    • Effect of rigor temperature and frozen storage on functional properties of hot-boned manufacturing beef
    • Farouk MM, Swan JE. 1998a. Effect of rigor temperature and frozen storage on functional properties of hot-boned manufacturing beef. Meat Sci 49(2):233-247.
    • (1998) Meat Sci , vol.49 , Issue.2 , pp. 233-247
    • Farouk, M.M.1    Swan, J.E.2
  • 10
    • 0032334657 scopus 로고    scopus 로고
    • Effect of muscle condition before freezing and simulated chemical changes during frozen storage on the pH and colour of beef
    • Farouk MM, Swan JE. 1998b. Effect of muscle condition before freezing and simulated chemical changes during frozen storage on the pH and colour of beef. Meat Sci 50:245-56.
    • (1998) Meat Sci , vol.50 , pp. 245-256
    • Farouk, M.M.1    Swan, J.E.2
  • 11
    • 0013441316 scopus 로고    scopus 로고
    • Loss of protein functionality in frozen beef may be caused by interactions involving fat oxidation products and free amino groups
    • Krakow, Poland. Warsaw, Poland: Meat and Fat Research Institute
    • Farouk MM, Wieliczko K, Podmore C, Agnew MP, Frost DA. 2001. Loss of protein functionality in frozen beef may be caused by interactions involving fat oxidation products and free amino groups. Proc 47th ICoMST, Krakow, Poland. Vol 1. Warsaw, Poland: Meat and Fat Research Institute. p 282-3.
    • (2001) Proc 47th ICoMST , vol.1 , pp. 282-283
    • Farouk, M.M.1    Wieliczko, K.2    Podmore, C.3    Agnew, M.P.4    Frost, D.A.5
  • 13
    • 0028925570 scopus 로고
    • Protein destabilization at low temperatures
    • Franks F. 1995. Protein destabilization at low temperatures. Adv Prot Chem 46:105-39.
    • (1995) Adv Prot Chem , vol.46 , pp. 105-139
    • Franks, F.1
  • 15
    • 0002651982 scopus 로고
    • Rheology as a means of evaluating muscle functionality of processed foods
    • Hamann DD. 1988. Rheology as a means of evaluating muscle functionality of processed foods. Food Technol 42(6):66-71.
    • (1988) Food Technol , vol.42 , Issue.6 , pp. 66-71
    • Hamann, D.D.1
  • 16
    • 0001349832 scopus 로고
    • Instrumental methods for predicting seafood sensory texture quality
    • Kramer DE, Liston J, editors. Barking, Essex, England: Elsevier
    • Hamann DD, Lanier TC. 1987. Instrumental methods for predicting seafood sensory texture quality. In: Kramer DE, Liston J, editors. Seafood quality determination. Barking, Essex, England: Elsevier. p 123-36.
    • (1987) Seafood Quality Determination , pp. 123-136
    • Hamann, D.D.1    Lanier, T.C.2
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0033827809 scopus 로고    scopus 로고
    • Chemical, physical, and gel-forming properties of oxidized myofibrils and whey- and soy-protein isolates
    • Liu G, Xiong YL, Butterfield DA. 2000. Chemical, physical, and gel-forming properties of oxidized myofibrils and whey- and soy-protein isolates. J Food Sci 65:811-8.
    • (2000) J Food Sci , vol.65 , pp. 811-818
    • Liu, G.1    Xiong, Y.L.2    Butterfield, D.A.3
  • 19
    • 0001294231 scopus 로고
    • Denaturation of fish proteins during frozen storage
    • Fennema O, editor. Proteins at Low Temperatures. Washington, D.C.: American Chemical Society
    • Matsumoto JJ. 1979. Denaturation of fish proteins during frozen storage. In: Fennema O, editor. Proteins at low temperatures. Advances in Chemistry Series 180. Washington, D.C.: American Chemical Society. p 205-24.
    • (1979) Advances in Chemistry Series , vol.180 , pp. 205-224
    • Matsumoto, J.J.1
  • 20
    • 0000511437 scopus 로고
    • Effects of frozen storage on functionality of meat for processing
    • Miller AJ, Ackerman AS, Palumho SA. 1980. Effects of frozen storage on functionality of meat for processing. J Food Sci 45:1466-71.
    • (1980) J Food Sci , vol.45 , pp. 1466-1471
    • Miller, A.J.1    Ackerman, A.S.2    Palumho, S.A.3
  • 21
    • 0034057792 scopus 로고    scopus 로고
    • Preliminary analysis of amino acids at various locations along the m. longissimus dorsi in aged beef
    • Mullen AM, Stoeva S, Laib K, Gruebler G, Voelter W, Troy DJ. 2000. Preliminary analysis of amino acids at various locations along the m. longissimus dorsi in aged beef. Food Chem 69:461-5.
    • (2000) Food Chem , vol.69 , pp. 461-465
    • Mullen, A.M.1    Stoeva, S.2    Laib, K.3    Gruebler, G.4    Voelter, W.5    Troy, D.J.6
  • 22
    • 0000665651 scopus 로고
    • Theories of protein denaturation during frozen storage of fish flesh
    • Shenouda SYK. 1980. Theories of protein denaturation during frozen storage of fish flesh. Adv Food Res 26:275-311.
    • (1980) Adv Food Res , vol.26 , pp. 275-311
    • Shenouda, S.Y.K.1
  • 23
    • 84986465454 scopus 로고
    • Hydroxyl radical modification of fish muscle proteins
    • Srinivasan S, Hultin HO. 1995. Hydroxyl radical modification of fish muscle proteins. J Food Biochem 18:405-25.
    • (1995) J Food Biochem , vol.18 , pp. 405-425
    • Srinivasan, S.1    Hultin, H.O.2
  • 24
    • 84981389691 scopus 로고
    • Fabricated foodstuffs as multicomponent gels
    • Tolstoguzov VB, Braudo EE. 1983. Fabricated foodstuffs as multicomponent gels. J Texture Stud 14:183-221.
    • (1983) J Texture Stud , vol.14 , pp. 183-221
    • Tolstoguzov, V.B.1    Braudo, E.E.2
  • 25
    • 0002207238 scopus 로고
    • The structural and interfacial properties of food proteins in relation to their function in emulsions
    • Larsson K, Friberg SE, editors. New York, N.Y.: Marcel Dekker, Inc.
    • Tornberg E, Olsson A, Persson K. 1990. The structural and interfacial properties of food proteins in relation to their function in emulsions. In: Larsson K, Friberg SE, editors. Food emulsions. 2nd ed. New York, N.Y.: Marcel Dekker, Inc. p 247-325.
    • (1990) Food Emulsions. 2nd Ed. , pp. 247-325
    • Tornberg, E.1    Olsson, A.2    Persson, K.3
  • 26
    • 0002835660 scopus 로고    scopus 로고
    • Impacts of oxidation on muscle protein functionality
    • Xiong YL. 1996. Impacts of oxidation on muscle protein functionality. Proc Recip Meat Conf 49:79-86.
    • (1996) Proc Recip Meat Conf , vol.49 , pp. 79-86
    • Xiong, Y.L.1
  • 27
    • 84987290994 scopus 로고
    • Changes in protein solubility and gelation properties of chicken myofibrils during storage
    • Xiong YL, Brekke CJ. 1989. Changes in protein solubility and gelation properties of chicken myofibrils during storage. J Food Sci 54(5):1141-6.
    • (1989) J Food Sci , vol.54 , Issue.5 , pp. 1141-1146
    • Xiong, Y.L.1    Brekke, C.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.