메뉴 건너뛰기




Volumn 4, Issue 1, 2012, Pages

Effect of pretreatments on chemical compositions of mince from Nile tilapia (Oreochromis niloticus) and fishy odor development in protein hydrolysate

Author keywords

Fishy odor; Fortification; Lipid oxidation; Nile tilapia; Protein hydrolysate

Indexed keywords

OREOCHROMIS NILOTICUS;

EID: 84885679821     PISSN: 20084935     EISSN: 20086970     Source Type: Journal    
DOI: 10.1186/2008-6970-4-7     Document Type: Article
Times cited : (14)

References (44)
  • 1
    • 0033041632 scopus 로고    scopus 로고
    • Effect of plant extracts on the oxidative stability of sunflower oil and emulsion
    • COI: 1:CAS:528:DyaK1MXms1Wqtw%3D%3D
    • Abdalla AE, Roozen JP: Effect of plant extracts on the oxidative stability of sunflower oil and emulsion.Food Chem 1999, 64:323–329.
    • (1999) Food Chem , vol.64 , pp. 323-329
    • Abdalla, A.E.1    Roozen, J.P.2
  • 2
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • COI: 1:CAS:528:DyaE1MXlvFWnsbw%3D
    • Adler-Nissen J: Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid.J Agric Food Chem 1979, 27:1256–1262.
    • (1979) J Agric Food Chem , vol.27 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 3
    • 0000740941 scopus 로고
    • Effect of haemoglobin and ferritin on lipid oxidation in raw and cooked muscle systems
    • COI: 1:CAS:528:DyaL2sXltFCntr8%3D
    • Apte S, Morrissey P: Effect of haemoglobin and ferritin on lipid oxidation in raw and cooked muscle systems.Food Chem 1987, 25:127–134.
    • (1987) Food Chem , vol.25 , pp. 127-134
    • Apte, S.1    Morrissey, P.2
  • 4
    • 67349127237 scopus 로고    scopus 로고
    • Association of Official Chemists, Maryland:
    • AOAC: Official Methods of Analysis. Association of Official Chemists, Maryland; 2000.
    • (2000) Official Methods of Analysis
    • AOAC1
  • 5
    • 0031462866 scopus 로고    scopus 로고
    • Physicochemical changes in Pacific whiting muscle proteins during iced storage
    • COI: 1:CAS:528:DyaK2sXlvFegtbw%3D
    • Benjakul S, Seymour TA, Morrissey MT, An H: Physicochemical changes in Pacific whiting muscle proteins during iced storage.J Food Sci 1997, 62:729–733.
    • (1997) J Food Sci , vol.62 , pp. 729-733
    • Benjakul, S.1    Seymour, T.A.2    Morrissey, M.T.3    An, H.4
  • 6
    • 0000717975 scopus 로고    scopus 로고
    • Protein hydrolysates from Pacific whiting solid wastes
    • COI: 1:CAS:528:DyaK2sXmtFSgsb0%3D
    • Benjakul S, Morrissey MT: Protein hydrolysates from Pacific whiting solid wastes.J Agric Food Chem 1997, 45:3423–3430.
    • (1997) J Agric Food Chem , vol.45 , pp. 3423-3430
    • Benjakul, S.1    Morrissey, M.T.2
  • 7
    • 0017872475 scopus 로고
    • Microsomal lipid peroxidation
    • COI: 1:CAS:528:DyaE1MXltVajsw%3D%3D
    • Buege JA, Aust SD: Microsomal lipid peroxidation.Methods Enzymol 1978, 52:302–310.
    • (1978) Methods Enzymol , vol.52 , pp. 302-310
    • Buege, J.A.1    Aust, S.D.2
  • 8
    • 20444391056 scopus 로고    scopus 로고
    • Changes of pigments and color in sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) muscle during iced storage
    • COI: 1:CAS:528:DC%2BD2MXkvFWrtbo%3D
    • Chaijan M, Benjakul S, Visessanguan W, Faustman C: Changes of pigments and color in sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) muscle during iced storage.Food Chem 2005, 93:607–617.
    • (2005) Food Chem , vol.93 , pp. 607-617
    • Chaijan, M.1    Benjakul, S.2    Visessanguan, W.3    Faustman, C.4
  • 9
    • 3242721531 scopus 로고    scopus 로고
    • Effect of ascorbic acid with tumbling on lipid oxidation of precooked roast beef
    • COI: 1:CAS:528:DC%2BD2cXmtlCgt7Y%3D
    • Cheng EH, Ockerman HW: Effect of ascorbic acid with tumbling on lipid oxidation of precooked roast beef.J Muscle Foods 2004, 15:83–93.
    • (2004) J Muscle Foods , vol.15 , pp. 83-93
    • Cheng, E.H.1    Ockerman, H.W.2
  • 10
    • 0000093464 scopus 로고
    • An absorption apparatus for the micro-determination of certain volatile substances: the micro-determination of ammonia
    • COI: 1:CAS:528:DyaA3sXktlShsw%3D%3D
    • Conway EJ, Byrne A: An absorption apparatus for the micro-determination of certain volatile substances: the micro-determination of ammonia.Biochem J 1933, 27:419.
    • (1933) Biochem J , vol.27 , pp. 419
    • Conway, E.J.1    Byrne, A.2
  • 11
    • 0033476219 scopus 로고    scopus 로고
    • Lipids and meat quality: lipolysis, oxidation, Maillard reaction and flavour
    • COI: 1:CAS:528:DC%2BD3cXivVKntA%3D%3D
    • Gandemer G: Lipids and meat quality: lipolysis, oxidation, Maillard reaction and flavour.Sci Aliments 1999, 19:439–458.
    • (1999) Sci Aliments , vol.19 , pp. 439-458
    • Gandemer, G.1
  • 12
    • 84987321944 scopus 로고
    • Vacuum packaging, ascorbic acid and frozen storage effects on heme and non-heme iron content of mackerel
    • COI: 1:CAS:528:DyaK3sXhs1OrtL8%3D
    • Gomez-Basauri JV, Regenstein JM: Vacuum packaging, ascorbic acid and frozen storage effects on heme and non-heme iron content of mackerel.J Food Sci 1992, 57:1337–1339.
    • (1992) J Food Sci , vol.57 , pp. 1337-1339
    • Gomez-Basauri, J.V.1    Regenstein, J.M.2
  • 13
    • 0030297237 scopus 로고    scopus 로고
    • Microbiological spoilage of fish and fish products
    • COI: 1:STN:280:DyaK2s%2FntVyrtQ%3D%3D
    • Gram L, Huss HH: Microbiological spoilage of fish and fish products.Int J Food Microbiol 1996, 33:121–137.
    • (1996) Int J Food Microbiol , vol.33 , pp. 121-137
    • Gram, L.1    Huss, H.H.2
  • 15
    • 79251528597 scopus 로고    scopus 로고
    • Impact of citric acid and calcium ions on acid solubilization of mechanically separated turkey meat: Effect on lipid and pigment content
    • COI: 1:CAS:528:DC%2BC3MXis1egtLY%3D
    • Hrynets Y, Omana DA, Xu Y, Betti M: Impact of citric acid and calcium ions on acid solubilization of mechanically separated turkey meat: Effect on lipid and pigment content.Poultry Sci 2011, 90:458–466.
    • (2011) Poultry Sci , vol.90 , pp. 458-466
    • Hrynets, Y.1    Omana, D.A.2    Xu, Y.3    Betti, M.4
  • 16
    • 0002246624 scopus 로고
    • Seafood: chemistry, processing technology and quality
    • Botta J, (ed), Blackie Academic, Glasgow:
    • Hultin HO: Seafood: chemistry, processing technology and quality. In Shahidi F. Edited by: Botta J. Blackie Academic, Glasgow; 1994:49–74.
    • (1994) Shahidi F , pp. 49-74
    • Hultin, H.O.1
  • 18
    • 78751704180 scopus 로고    scopus 로고
    • The effects of pretreatments on antioxidative activities of protein hydrolysate from the muscle of brownstripe red snapper (Lutjanus vitta)
    • COI: 1:CAS:528:DC%2BC3MXhtVWhu7c%3D
    • Khantaphant S, Benjakul S, Ghomi MR: The effects of pretreatments on antioxidative activities of protein hydrolysate from the muscle of brownstripe red snapper (Lutjanus vitta).LWT- Food Sci Technol 2011, 44:1139–1148.
    • (2011) LWT- Food Sci Technol , vol.44 , pp. 1139-1148
    • Khantaphant, S.1    Benjakul, S.2    Ghomi, M.R.3
  • 19
    • 0001748740 scopus 로고    scopus 로고
    • Effect of heat denaturation on the pro-oxidative activity of metmyoglobin in linoleic acid emulsions
    • COI: 1:CAS:528:DyaK2sXitVKmtg%3D%3D
    • Kristensen L, Andersen HJ: Effect of heat denaturation on the pro-oxidative activity of metmyoglobin in linoleic acid emulsions.J Agric Food Chem 1997, 45:7–13.
    • (1997) J Agric Food Chem , vol.45 , pp. 7-13
    • Kristensen, L.1    Andersen, H.J.2
  • 20
    • 0034117422 scopus 로고    scopus 로고
    • Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases
    • COI: 1:CAS:528:DC%2BD3cXhsVWjtr0%3D
    • Kristinsson HG, Rasco BA: Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases.J Agric Food Chem 2000, 48:657–666.
    • (2000) J Agric Food Chem , vol.48 , pp. 657-666
    • Kristinsson, H.G.1    Rasco, B.A.2
  • 21
    • 19444381148 scopus 로고    scopus 로고
    • A comparative study between acid-and alkali-aided processing and surimi processing for the recovery of proteins from channel catfish muscle
    • COI: 1:CAS:528:DC%2BD2MXkslyrsLc%3D
    • Kristinsson HG, Theodore AE, Demir N, Ingadottir B: A comparative study between acid-and alkali-aided processing and surimi processing for the recovery of proteins from channel catfish muscle.J Food Sci 2005, 70:C298-C306.
    • (2005) J Food Sci , vol.70 , pp. C298-C306
    • Kristinsson, H.G.1    Theodore, A.E.2    Demir, N.3    Ingadottir, B.4
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • COI: 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4.Nature 1970, 227:680–685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 17144427288 scopus 로고    scopus 로고
    • Separation of membranes from acid-solubilized fish muscle proteins with the aid of calcium ions and organic acids
    • COI: 1:CAS:528:DC%2BD2MXitlSisbs%3D
    • Liang Y, Hultin HO: Separation of membranes from acid-solubilized fish muscle proteins with the aid of calcium ions and organic acids.J Agric Food Chem 2005, 53:3008–3016.
    • (2005) J Agric Food Chem , vol.53 , pp. 3008-3016
    • Liang, Y.1    Hultin, H.O.2
  • 24
    • 30544451083 scopus 로고    scopus 로고
    • Separation of muscle membrane from alkali-solubilized fish muscle proteins
    • COI: 1:CAS:528:DC%2BD2MXht1eitrjO
    • Liang Y, Hultin HO: Separation of muscle membrane from alkali-solubilized fish muscle proteins.J Agric Food Chem 2005, 53:10012–10017.
    • (2005) J Agric Food Chem , vol.53 , pp. 10012-10017
    • Liang, Y.1    Hultin, H.O.2
  • 26
    • 84865357058 scopus 로고    scopus 로고
    • Optimization of enzymatic hydrolysis of visceral waste proteins of beluga sturgeon Huso huso using Alcalase
    • Ovissipour M, Taghiof M, Motamedzadegan A, Rasco B, Molla AE: Optimization of enzymatic hydrolysis of visceral waste proteins of beluga sturgeon Huso huso using Alcalase.Int Aquat Res 2009, 1:31–38.
    • (2009) Int Aquat Res , vol.1 , pp. 31-38
    • Ovissipour, M.1    Taghiof, M.2    Motamedzadegan, A.3    Rasco, B.4    Molla, A.E.5
  • 27
    • 64149104095 scopus 로고    scopus 로고
    • Effect of various antioxidants on the oxidative stability of acid and alkali solubilized muscle protein isolates
    • COI: 1:CAS:528:DC%2BD1MXotVSitbs%3D
    • Raghavan S, Hultin HO: Effect of various antioxidants on the oxidative stability of acid and alkali solubilized muscle protein isolates.J Food Biochem 2009, 33:163–175.
    • (2009) J Food Biochem , vol.33 , pp. 163-175
    • Raghavan, S.1    Hultin, H.O.2
  • 28
    • 40549121909 scopus 로고    scopus 로고
    • Antioxidative efficacy of alkali-treated tilapia protein hydrolysates: a comparative study of five enzymes
    • COI: 1:CAS:528:DC%2BD1cXhsVKltrk%3D
    • Raghavan S, Kristinsson HG: Antioxidative efficacy of alkali-treated tilapia protein hydrolysates: a comparative study of five enzymes.J Agric Food Chem 2008, 56:1434–1441.
    • (2008) J Agric Food Chem , vol.56 , pp. 1434-1441
    • Raghavan, S.1    Kristinsson, H.G.2
  • 29
    • 58149359080 scopus 로고    scopus 로고
    • Radical scavenging and reducing ability of tilapia (Oreochromis niloticus) protein hydrolysates
    • COI: 1:CAS:528:DC%2BD1cXhtF2ju7fN
    • Raghavan S, Kristinsson HG, Leeuwenburgh C: Radical scavenging and reducing ability of tilapia (Oreochromis niloticus) protein hydrolysates.J Agric Food Chem 2008, 56:10359–10367.
    • (2008) J Agric Food Chem , vol.56 , pp. 10359-10367
    • Raghavan, S.1    Kristinsson, H.G.2    Leeuwenburgh, C.3
  • 30
    • 47949083218 scopus 로고    scopus 로고
    • Biochemical and gelling properties of tilapia surimi and protein recovered using an acid-alkaline process
    • COI: 1:CAS:528:DC%2BD1cXovFyjtrY%3D
    • Rawdkuen S, Sai-Ut S, Khamsorn S, Chaijan M, Benjakul S: Biochemical and gelling properties of tilapia surimi and protein recovered using an acid-alkaline process.Food Chem 2009, 112:112–119.
    • (2009) Food Chem , vol.112 , pp. 112-119
    • Rawdkuen, S.1    Sai-Ut, S.2    Khamsorn, S.3    Chaijan, M.4    Benjakul, S.5
  • 31
    • 0033851262 scopus 로고    scopus 로고
    • Effect of pH on lipid oxidation using trout hemolysate as a catalyst: a possible role for deoxyhemoglobin
    • COI: 1:CAS:528:DC%2BD3cXksleiurw%3D
    • Richards MP, Hultin HO: Effect of pH on lipid oxidation using trout hemolysate as a catalyst: a possible role for deoxyhemoglobin.J Agric Food Chem 2000, 48:3141–3147.
    • (2000) J Agric Food Chem , vol.48 , pp. 3141-3147
    • Richards, M.P.1    Hultin, H.O.2
  • 32
    • 0000451299 scopus 로고
    • The biuret reaction in the determination of serum proteins
    • COI: 1:CAS:528:DyaH3cXkslOmtA%3D%3D
    • Robinson HW, Hogden CG: The biuret reaction in the determination of serum proteins.J Biol Chem 1940, 135:727.
    • (1940) J Biol Chem , vol.135 , pp. 727
    • Robinson, H.W.1    Hogden, C.G.2
  • 33
    • 84986450169 scopus 로고
    • Measurement and content of nonheme and total iron in muscle
    • COI: 1:CAS:528:DyaL38XhvFOqu78%3D
    • Schricker B, Miller D, Stouffer J: Measurement and content of nonheme and total iron in muscle.J Food Sci 1982, 47:740–743.
    • (1982) J Food Sci , vol.47 , pp. 740-743
    • Schricker, B.1    Miller, D.2    Stouffer, J.3
  • 35
    • 0029029764 scopus 로고
    • Production and characteristics of protein hydrolysates from capelin (Mallotus villosus)
    • COI: 1:CAS:528:DyaK2MXlvFSqsr0%3D
    • Shahidi F, Han XQ, Synowiecki J: Production and characteristics of protein hydrolysates from capelin (Mallotus villosus).Food Chem 1995, 53:285–293.
    • (1995) Food Chem , vol.53 , pp. 285-293
    • Shahidi, F.1    Han, X.Q.2    Synowiecki, J.3
  • 36
    • 0036649939 scopus 로고    scopus 로고
    • Partitioning of ρ-tocopherol in aqueous mixtures of TAG and isolated muscle membranes
    • COI: 1:CAS:528:DC%2BD38XlsFCgtrw%3D
    • Sigfusson H, Hultin HO: Partitioning of ρ-tocopherol in aqueous mixtures of TAG and isolated muscle membranes.J Am Oil Chem 2002, 79:691–697.
    • (2002) J Am Oil Chem , vol.79 , pp. 691-697
    • Sigfusson, H.1    Hultin, H.O.2
  • 37
    • 25844525770 scopus 로고    scopus 로고
    • Lipid oxidations in ordinary and dark muscles of fish:influences on rancid off odor development and color darkening of yellowtail flesh during ice storage
    • COI: 1:CAS:528:DC%2BD2MXhtVOqsLfK
    • Sohn JH, Taki Y, Ushio H, Kohata T, Shioya I, Ohshima T: Lipid oxidations in ordinary and dark muscles of fish:influences on rancid off odor development and color darkening of yellowtail flesh during ice storage.J Food Sci 2005, 70:s490-s496.
    • (2005) J Food Sci , vol.70 , pp. s490-s496
    • Sohn, J.H.1    Taki, Y.2    Ushio, H.3    Kohata, T.4    Shioya, I.5    Ohshima, T.6
  • 38
    • 85008106450 scopus 로고
    • Characterization of phosvitin and phosphopeptides of rainbow trout (Salmo gairdnerii) eggs
    • COI: 1:CAS:528:DyaL2MXlsFOltLY%3D
    • Suzuki T, Suyama M: Characterization of phosvitin and phosphopeptides of rainbow trout (Salmo gairdnerii) eggs.Bull Jpn Soc Sci Fish 1985, 51:1287–1292.
    • (1985) Bull Jpn Soc Sci Fish , vol.51 , pp. 1287-1292
    • Suzuki, T.1    Suyama, M.2
  • 39
    • 65849145033 scopus 로고    scopus 로고
    • Characterization and ACE-Inhibitory activity of amaranth proteins
    • COI: 1:CAS:528:DC%2BD1MXntFWisr8%3D
    • Tiengo A, Faria M, Netto FM: Characterization and ACE-Inhibitory activity of amaranth proteins.J Food Sci 2009, 74:H121-H126.
    • (2009) J Food Sci , vol.74 , pp. H121-H126
    • Tiengo, A.1    Faria, M.2    Netto, F.M.3
  • 40
    • 79952097541 scopus 로고    scopus 로고
    • Effect of myoglobin from eastern little tuna muscle on lipid oxidation of washed Asian seabass mince at different pH conditions
    • COI: 1:CAS:528:DC%2BC3MXjsVaisbw%3D
    • Thiansilakul Y, Benjakul S, Richards MP: Effect of myoglobin from eastern little tuna muscle on lipid oxidation of washed Asian seabass mince at different pH conditions.J Food Sci 2011, 76:C242-C249.
    • (2011) J Food Sci , vol.76 , pp. C242-C249
    • Thiansilakul, Y.1    Benjakul, S.2    Richards, M.P.3
  • 41
    • 79955827146 scopus 로고    scopus 로고
    • Characteristics of film based on protein isolate from red tilapia muscle with negligible yellow discoloration
    • COI: 1:CAS:528:DC%2BC3MXmtFCku7s%3D
    • Tongnuanchan P, Benjakul S, Prodpran T, Songtipya P: Characteristics of film based on protein isolate from red tilapia muscle with negligible yellow discoloration.Int J Biol Macromol 2011, 48:758–767.
    • (2011) Int J Biol Macromol , vol.48 , pp. 758-767
    • Tongnuanchan, P.1    Benjakul, S.2    Prodpran, T.3    Songtipya, P.4
  • 42
    • 37549048538 scopus 로고    scopus 로고
    • Hemoglobin-mediated lipid oxidation of protein isolates obtained from cod and haddock white muscle as affected by citric acid, calcium chloride and pH
    • COI: 1:CAS:528:DC%2BD1cXitVGktQ%3D%3D
    • Vareltzis P, Hultin HO, Autio WR: Hemoglobin-mediated lipid oxidation of protein isolates obtained from cod and haddock white muscle as affected by citric acid, calcium chloride and pH.Food Chem 2008, 108:64–74.
    • (2008) Food Chem , vol.108 , pp. 64-74
    • Vareltzis, P.1    Hultin, H.O.2    Autio, W.R.3
  • 43
    • 84857042059 scopus 로고    scopus 로고
    • Lipid oxidation and fishy odour development in protein hydrolysate from Nile tilapia (Oreochromis niloticus) muscle as affected by freshness and antioxidants
    • COI: 1:CAS:528:DC%2BC38Xit1WnsLw%3D
    • Yarnpakdee S, Benjakul S, Nalinanon S, Kristinsson HG: Lipid oxidation and fishy odour development in protein hydrolysate from Nile tilapia (Oreochromis niloticus) muscle as affected by freshness and antioxidants.Food Chem 2012, 132:1781–1788.
    • (2012) Food Chem , vol.132 , pp. 1781-1788
    • Yarnpakdee, S.1    Benjakul, S.2    Nalinanon, S.3    Kristinsson, H.G.4
  • 44
    • 77952428375 scopus 로고    scopus 로고
    • Production and characterization of Angiotensin converting enzyme (ACE) inhibitory peptides from apricot (Prunus armeniaca L.) kernel protein hydrolysate
    • COI: 1:CAS:528:DC%2BC3cXkslSmsb8%3D
    • Zhu Z, Qiu N, Yi J: Production and characterization of Angiotensin converting enzyme (ACE) inhibitory peptides from apricot (Prunus armeniaca L.) kernel protein hydrolysate.Eur Food Res Technol 2010, 231:13–19.
    • (2010) Eur Food Res Technol , vol.231 , pp. 13-19
    • Zhu, Z.1    Qiu, N.2    Yi, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.