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Volumn 113, Issue 1, 2009, Pages 61-70

Enhancement of gel strength of bigeye snapper (Priacanthus tayenus) surimi using oxidised phenolic compounds

Author keywords

Bigeye snapper; Cross linking; Gelation; Oxygenation; Phenolic compounds; Quinone; Surimi

Indexed keywords

AMINO ACID; CAFFEIC ACID; CATECHIN; FERULIC ACID; MYOSIN ADENOSINE TRIPHOSPHATASE; PHENOL DERIVATIVE; PROTEIN; TANNIN;

EID: 52949097180     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2008.07.039     Document Type: Article
Times cited : (169)

References (37)
  • 1
    • 84872887342 scopus 로고    scopus 로고
    • Asen, S., Stewart, R. N., & Norris, K. H. (1979). Stable foods and beverages containing the anthocyanin, peonidin, 3-(dicaffeylsophoroside)-5-glucoside. United States Patent 4172902.
    • Asen, S., Stewart, R. N., & Norris, K. H. (1979). Stable foods and beverages containing the anthocyanin, peonidin, 3-(dicaffeylsophoroside)-5-glucoside. United States Patent 4172902.
  • 3
    • 0031462866 scopus 로고    scopus 로고
    • Physicochemical changes in Pacific whiting muscle proteins during iced storage
    • Benjakul S., Seymour T.S., Morrissey M.T., and An H. Physicochemical changes in Pacific whiting muscle proteins during iced storage. Journal of Food Science 62 (1997) 729-733
    • (1997) Journal of Food Science , vol.62 , pp. 729-733
    • Benjakul, S.1    Seymour, T.S.2    Morrissey, M.T.3    An, H.4
  • 4
    • 0037227661 scopus 로고    scopus 로고
    • Transglutaminase-mediated setting in bigeye snapper surimi
    • Benjakul S., and Visessanguan W. Transglutaminase-mediated setting in bigeye snapper surimi. Food Research International 36 (2003) 253-266
    • (2003) Food Research International , vol.36 , pp. 253-266
    • Benjakul, S.1    Visessanguan, W.2
  • 5
    • 0035730743 scopus 로고    scopus 로고
    • Gel properties of bigeye snapper (Priacanthus tayenus) surimi as affected by setting and porcine plasma protein
    • Benjakul S., Visessanguan W., and Srivilai C. Gel properties of bigeye snapper (Priacanthus tayenus) surimi as affected by setting and porcine plasma protein. Journal of Food Quality 24 (2001) 453-471
    • (2001) Journal of Food Quality , vol.24 , pp. 453-471
    • Benjakul, S.1    Visessanguan, W.2    Srivilai, C.3
  • 6
    • 0037388169 scopus 로고    scopus 로고
    • Changes in physicochemical properties and gel-forming ability of lizardfish (Saurida tumbil) during post-mortem storage in ice
    • Benjakul S., Visessanguan W., and Tueksuban J. Changes in physicochemical properties and gel-forming ability of lizardfish (Saurida tumbil) during post-mortem storage in ice. Food Chemistry 80 (2003) 535-544
    • (2003) Food Chemistry , vol.80 , pp. 535-544
    • Benjakul, S.1    Visessanguan, W.2    Tueksuban, J.3
  • 9
    • 0035117563 scopus 로고    scopus 로고
    • Structural features of procyanidin interactions with salivary proteins
    • De Freitas V., and Mateus N. Structural features of procyanidin interactions with salivary proteins. Journal of Agricultural and Food Chemistry 49 (2001) 940-945
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , pp. 940-945
    • De Freitas, V.1    Mateus, N.2
  • 14
    • 85010163337 scopus 로고
    • Mechanism, behavior and cross linkages of heat-induced myosin gel
    • Hamada M. Mechanism, behavior and cross linkages of heat-induced myosin gel. Nippon Suisan Gakkaishi 58 (1992) 89-93
    • (1992) Nippon Suisan Gakkaishi , vol.58 , pp. 89-93
    • Hamada, M.1
  • 15
    • 0003304907 scopus 로고
    • Vegetable tannins revisited
    • Phillipson J.D., Ayres D.C., and Baxter H. (Eds), Cambridge, Cambridge University Press pp. 230
    • Haslam E. Vegetable tannins revisited. In: Phillipson J.D., Ayres D.C., and Baxter H. (Eds). Plant polyphenols (1989), Cambridge, Cambridge University Press pp. 230
    • (1989) Plant polyphenols
    • Haslam, E.1
  • 16
    • 0001221912 scopus 로고
    • Contribution of hydrophobicity, net charge and sulfhydryl groups to thermal properties of ovalbumin
    • Hayakawa S., and Nakai S. Contribution of hydrophobicity, net charge and sulfhydryl groups to thermal properties of ovalbumin. Canadian Institute of Food Science Technology Journal 18 (1985) 290-295
    • (1985) Canadian Institute of Food Science Technology Journal , vol.18 , pp. 290-295
    • Hayakawa, S.1    Nakai, S.2
  • 17
    • 0033559516 scopus 로고    scopus 로고
    • Yates III, J. R. mass spectrometric analysis of catechol-histidine adducts from insect cuticle
    • Kerwin J.L., Turecek F., Xu R., Kramer K.J., Hopkins T.L., and Gatlin C.L. Yates III, J. R. mass spectrometric analysis of catechol-histidine adducts from insect cuticle. Analytical Biochemistry 268 (1999) 229-237
    • (1999) Analytical Biochemistry , vol.268 , pp. 229-237
    • Kerwin, J.L.1    Turecek, F.2    Xu, R.3    Kramer, K.J.4    Hopkins, T.L.5    Gatlin, C.L.6
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0000691728 scopus 로고
    • Functional properties of surimi
    • Lanier T.C. Functional properties of surimi. Food Technology 3 (1986) 107-114
    • (1986) Food Technology , vol.3 , pp. 107-114
    • Lanier, T.C.1
  • 20
    • 0001554239 scopus 로고    scopus 로고
    • Surimi gelation chemistry
    • Park J.W. (Ed), Marcel Dekker, New York, USA
    • Lanier T.C. Surimi gelation chemistry. In: Park J.W. (Ed). Surimi and surimi seafood (2000), Marcel Dekker, New York, USA 237-265
    • (2000) Surimi and surimi seafood , pp. 237-265
    • Lanier, T.C.1
  • 23
    • 7444226886 scopus 로고    scopus 로고
    • Extraction and analysis of phenolics in food
    • Naczk M., and Shahidi F. Extraction and analysis of phenolics in food. Journal of Chromatography A 1054 (2004) 95-111
    • (2004) Journal of Chromatography A , vol.1054 , pp. 95-111
    • Naczk, M.1    Shahidi, F.2
  • 24
    • 0000323022 scopus 로고
    • Chemistry of surimi gelation
    • Lanier T.C., and Lee C.M. (Eds), Marcel Dekker, New York, USA
    • Niwa E. Chemistry of surimi gelation. In: Lanier T.C., and Lee C.M. (Eds). Surimi technology (1992), Marcel Dekker, New York, USA 389-428
    • (1992) Surimi technology , pp. 389-428
    • Niwa, E.1
  • 25
    • 0034926162 scopus 로고    scopus 로고
    • Significance and applications of phenolic compounds in the production and quality of milk and dairy products
    • O'Connell J.E., and Fox P.F. Significance and applications of phenolic compounds in the production and quality of milk and dairy products. International Dairy Journal 11 (2001) 103-120
    • (2001) International Dairy Journal , vol.11 , pp. 103-120
    • O'Connell, J.E.1    Fox, P.F.2
  • 26
    • 84872883305 scopus 로고    scopus 로고
    • Prigent, S. (2005). Interactions of phenolic compounds with globular proteins and their effects on food related functional properties, Ph.D. thesis. The Netherlands: Wageningen University.
    • Prigent, S. (2005). Interactions of phenolic compounds with globular proteins and their effects on food related functional properties, Ph.D. thesis. The Netherlands: Wageningen University.
  • 28
    • 34548573053 scopus 로고    scopus 로고
    • Whey protein concentrate: Autolysis inhibition and effects on the gel properties of surimi prepared from tropical fish
    • Rawdkuen S., and Benjakul S. Whey protein concentrate: Autolysis inhibition and effects on the gel properties of surimi prepared from tropical fish. Food Chemistry 106 (2008) 1077-1084
    • (2008) Food Chemistry , vol.106 , pp. 1077-1084
    • Rawdkuen, S.1    Benjakul, S.2
  • 29
    • 0036768548 scopus 로고    scopus 로고
    • Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid
    • Rawel H.M., Rohn S., Kruse H.P., and Kroll J. Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid. Food Chemistry 78 (2002) 443-455
    • (2002) Food Chemistry , vol.78 , pp. 443-455
    • Rawel, H.M.1    Rohn, S.2    Kruse, H.P.3    Kroll, J.4
  • 30
    • 0000120207 scopus 로고
    • Cysteine as an inhibitor of enzymatic browning. 1. Isolation and characterization of addition compounds formed during oxidation of phenolics by apple polyphenol oxidase
    • Richard F.C., Goupy P.M., Nicolas J.J., Lacombe J.M., and Pavia A.A. Cysteine as an inhibitor of enzymatic browning. 1. Isolation and characterization of addition compounds formed during oxidation of phenolics by apple polyphenol oxidase. Journal of Agricultural and Food Chemistry 39 (1991) 841-847
    • (1991) Journal of Agricultural and Food Chemistry , vol.39 , pp. 841-847
    • Richard, F.C.1    Goupy, P.M.2    Nicolas, J.J.3    Lacombe, J.M.4    Pavia, A.A.5
  • 31
    • 0000451299 scopus 로고
    • The biuret reaction in the determination of serum protein. I. A study of condition necessary for the production of the stable colour which bears a quantitative relationship to the protein concentration
    • Robinson H.W., and Hodgen C.G. The biuret reaction in the determination of serum protein. I. A study of condition necessary for the production of the stable colour which bears a quantitative relationship to the protein concentration. Journal of Biological Chemistry 135 (1940) 707-725
    • (1940) Journal of Biological Chemistry , vol.135 , pp. 707-725
    • Robinson, H.W.1    Hodgen, C.G.2
  • 32
    • 0030265379 scopus 로고    scopus 로고
    • Phenolic protein interactions in relation to the gelation properties of canola protein
    • Rubino M.I., Arntfield S.D., Nadon C.A., and Bernatsky A. Phenolic protein interactions in relation to the gelation properties of canola protein. Food Research International 29 (1996) 653-659
    • (1996) Food Research International , vol.29 , pp. 653-659
    • Rubino, M.I.1    Arntfield, S.D.2    Nadon, C.A.3    Bernatsky, A.4
  • 34
    • 0000468690 scopus 로고
    • Phenolics of apple, pear, and white grape juices and their changes with processing and storage-a review
    • Spanos G.A., and Wrolstad R.E. Phenolics of apple, pear, and white grape juices and their changes with processing and storage-a review. Journal of Agricultural and Food Chemistry 40 (1992) 1478-1487
    • (1992) Journal of Agricultural and Food Chemistry , vol.40 , pp. 1478-1487
    • Spanos, G.A.1    Wrolstad, R.E.2
  • 36
    • 0344013443 scopus 로고    scopus 로고
    • Plant phenolics as cross-linkers of gelatin gels and gelatin-based coacervates for use as food ingredients
    • Strauss G., and Gibson S.M. Plant phenolics as cross-linkers of gelatin gels and gelatin-based coacervates for use as food ingredients. Food Hydrocolloids 18 (2004) 81-89
    • (2004) Food Hydrocolloids , vol.18 , pp. 81-89
    • Strauss, G.1    Gibson, S.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.