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Volumn 77, Issue 4, 2012, Pages

Optimum Chopping Conditions for Alaska Pollock, Pacific Whiting, and Threadfin Bream Surimi Paste and Gel based on Rheological and Raman Spectroscopic Analysis

Author keywords

Alaska pollock; Comminution; Dynamic rheology; Gel preparation; Pacific whiting; Raman spectroscopy; Surimi; Threadfin bream

Indexed keywords

DISULFIDE; FISH PROTEIN; MYOSIN SUBFRAGMENT;

EID: 84862812285     PISSN: 00221147     EISSN: 17503841     Source Type: Journal    
DOI: 10.1111/j.1750-3841.2011.02608.x     Document Type: Article
Times cited : (43)

References (31)
  • 1
    • 0030829061 scopus 로고    scopus 로고
    • In situ investigation of protein structure in Pacific whiting surimi and gels using Raman sspectroscopy
    • Bouraoui M, Nakai S, Li-Chan E. 1997. In situ investigation of protein structure in Pacific whiting surimi and gels using Raman sspectroscopy. Food Res Int 30(1):65-72.
    • (1997) Food Res Int , vol.30 , Issue.1 , pp. 65-72
    • Bouraoui, M.1    Nakai, S.2    Li-Chan, E.3
  • 2
    • 0031433220 scopus 로고    scopus 로고
    • Structural changes in cod myosin after modification with formaldehyde or frozen storage
    • Careche M, Li-Chan ECY. 1997. Structural changes in cod myosin after modification with formaldehyde or frozen storage. J Food Sci 62(4):717-23.
    • (1997) J Food Sci , vol.62 , Issue.4 , pp. 717-723
    • Careche, M.1    Li-Chan, E.C.Y.2
  • 3
    • 0016756385 scopus 로고
    • Laser Raman spectroscopy new probe of myosin substructure
    • Carew EB, Asher IM, Stanley HE. 1975. Laser Raman spectroscopy new probe of myosin substructure. Science 188:933-6.
    • (1975) Science , vol.188 , pp. 933-936
    • Carew, E.B.1    Asher, I.M.2    Stanley, H.E.3
  • 4
    • 84862780811 scopus 로고    scopus 로고
    • Mackerel trypsin purified from defatted viscera by supercritical carbon dioxide. J Amino Acids 2011 Article ID 728082:
    • Chun B, Kishimura H, Nalinanon S, Klomklao S, Benjakul S. 2011. Mackerel trypsin purified from defatted viscera by supercritical carbon dioxide. J Amino Acids 2011 Article ID 728082:7 p.
    • (2011) , pp. 7
    • Chun, B.1    Kishimura, H.2    Nalinanon, S.3    Klomklao, S.4    Benjakul, S.5
  • 5
    • 0030239609 scopus 로고    scopus 로고
    • Chopping temperature effects on the characteristics and chilled storage of low- and high- fat pork bologna sausages
    • Colmenero FJ, Carrascosa AV, Barreto G, Fernández P. 1996. Chopping temperature effects on the characteristics and chilled storage of low- and high- fat pork bologna sausages. Meat Sci 44(1-2):1-9.
    • (1996) Meat Sci , vol.44 , Issue.1-2 , pp. 1-9
    • Colmenero, F.J.1    Carrascosa, A.V.2    Barreto, G.3    Fernández, P.4
  • 6
    • 84985398393 scopus 로고
    • Dynamic theological measurements of heat induced myosin gels; effect of ionic stregnth, protein concentration and addition of adenosine triphosphate or pyrophosphate
    • Egelandsdal B, Fretheim K, Samejima K. 1986. Dynamic theological measurements of heat induced myosin gels; effect of ionic stregnth, protein concentration and addition of adenosine triphosphate or pyrophosphate. J Sci Food Agric 37(9):915-26.
    • (1986) J Sci Food Agric , vol.37 , Issue.9 , pp. 915-926
    • Egelandsdal, B.1    Fretheim, K.2    Samejima, K.3
  • 7
    • 7444239069 scopus 로고    scopus 로고
    • Thermal sensitivity of fish proteins from various species on rheological properties of gel
    • Esturk O, Park JW, Thawornchinsombut S. 2004. Thermal sensitivity of fish proteins from various species on rheological properties of gel. J Food Sci 69(7):E412-6.
    • (2004) J Food Sci , vol.69 , Issue.7
    • Esturk, O.1    Park, J.W.2    Thawornchinsombut, S.3
  • 8
    • 33846872789 scopus 로고    scopus 로고
    • Rheological properties of selected fish paste as selected temperature pertaining to shaping of surimi-based products
    • Fukushima H, Okasaki E, Fukuda Y, Watabe S. 2007. Rheological properties of selected fish paste as selected temperature pertaining to shaping of surimi-based products. J Food Eng 81:492-9.
    • (2007) J Food Eng , vol.81 , pp. 492-499
    • Fukushima, H.1    Okasaki, E.2    Fukuda, Y.3    Watabe, S.4
  • 9
    • 0038573664 scopus 로고    scopus 로고
    • Thermal effects on fast skeletal myosins from Alaska pollock, white croaker, and rabbit in relation to gel formation
    • Fukushima H, Satoh Y, Nakaya M, Ishizaki S, Watabe S. 2003. Thermal effects on fast skeletal myosins from Alaska pollock, white croaker, and rabbit in relation to gel formation. J Food Sci 68(5):1573-7.
    • (2003) J Food Sci , vol.68 , Issue.5 , pp. 1573-1577
    • Fukushima, H.1    Satoh, Y.2    Nakaya, M.3    Ishizaki, S.4    Watabe, S.5
  • 10
    • 28444467468 scopus 로고    scopus 로고
    • Rheological properties of fast skeletal myosin rod and light meromyosin from walleye pollack and white croaker: contribution of myosin fragments to thermal gel formation
    • Fukushima H, Satoh Y, Yoon SH, Togashi M, Nakaya M, Watabe S. 2005. Rheological properties of fast skeletal myosin rod and light meromyosin from walleye pollack and white croaker: contribution of myosin fragments to thermal gel formation. J Agric Food Chem 53:9193-8.
    • (2005) J Agric Food Chem , vol.53 , pp. 9193-9198
    • Fukushima, H.1    Satoh, Y.2    Yoon, S.H.3    Togashi, M.4    Nakaya, M.5    Watabe, S.6
  • 11
    • 51749125660 scopus 로고    scopus 로고
    • Thermal stability of fish natural actomyosin affects reactivity to cross-linking by microbial and fish transglutaminases
    • Hemung B, Li-Chan ECY, Yongsawatdigul J. 2008. Thermal stability of fish natural actomyosin affects reactivity to cross-linking by microbial and fish transglutaminases. Food Chem 111:439-46.
    • (2008) Food Chem , vol.111 , pp. 439-446
    • Hemung, B.1    Li-Chan, E.C.Y.2    Yongsawatdigul, J.3
  • 12
    • 84986468539 scopus 로고
    • Formulation and chopping temperature effects on beef frankfurters
    • 67
    • Hensley JL, Hand LW. 1995. Formulation and chopping temperature effects on beef frankfurters. J Food Sci 60(1):55-7, 67.
    • (1995) J Food Sci , vol.60 , Issue.1 , pp. 55-57
    • Hensley, J.L.1    Hand, L.W.2
  • 13
    • 45849088425 scopus 로고    scopus 로고
    • Raman spectroscopy for monitoring protein structure in muscle food systems
    • Herrero AM. 2008. Raman spectroscopy for monitoring protein structure in muscle food systems. Crit Rev Food Sci 48:512-23.
    • (2008) Crit Rev Food Sci , vol.48 , pp. 512-523
    • Herrero, A.M.1
  • 14
    • 0012388642 scopus 로고
    • Effect of temperature on the rate for the setting of meat pastes from Alaska Pollack, white croaker and tilapia
    • Kato N, Hashimoto A, Nozaki H, Arai K. 1984. Effect of temperature on the rate for the setting of meat pastes from Alaska Pollack, white croaker and tilapia. B Jpn Soc Sci Fish 50(12):2103-8.
    • (1984) B Jpn Soc Sci Fish , vol.50 , Issue.12 , pp. 2103-2108
    • Kato, N.1    Hashimoto, A.2    Nozaki, H.3    Arai, K.4
  • 15
    • 77449139338 scopus 로고    scopus 로고
    • Comparative study on thermal stability of trypsin from the pyloric ceca of threadfin hakeling (Laemonema longipes)
    • Kishimura H, Klomklao S, Nalinanon S, Benjakul S, Chun B, Adachi K. 2010. Comparative study on thermal stability of trypsin from the pyloric ceca of threadfin hakeling (Laemonema longipes). J Food Biochem 34:50-65.
    • (2010) J Food Biochem , vol.34 , pp. 50-65
    • Kishimura, H.1    Klomklao, S.2    Nalinanon, S.3    Benjakul, S.4    Chun, B.5    Adachi, K.6
  • 16
    • 26844557071 scopus 로고    scopus 로고
    • Gel forming ability of tropical tilapia surimi as compared with Alaska pollock and Pacific whiting surimi
    • Klesk K, Yongsawatdigul J, Park JW. 2000. Gel forming ability of tropical tilapia surimi as compared with Alaska pollock and Pacific whiting surimi. J Aquat Food Prod Technol 9:91-104.
    • (2000) J Aquat Food Prod Technol , vol.9 , pp. 91-104
    • Klesk, K.1    Yongsawatdigul, J.2    Park, J.W.3
  • 17
    • 33748339636 scopus 로고    scopus 로고
    • Surimi gelation chemistry
    • Park JW, editor. 2nd ed. Boca Raton, FL: CRC Press.
    • Lanier TC, Carvajal P, Yongsawatdigul J. 2005. Surimi gelation chemistry. In: Park JW, editor. Surimi and surimi seafood. 2nd ed. Boca Raton, FL: CRC Press. pp. 435-89.
    • (2005) Surimi and surimi seafood , pp. 435-489
    • Lanier, T.C.1    Carvajal, P.2    Yongsawatdigul, J.3
  • 18
    • 84862780813 scopus 로고
    • Development of methods for quality and functionality assesment of surimi and mince fish to be used in gel type food products. Anchorage, AK: Report to Alaska Fisheries Development Foundation, Inc
    • Lanier TC, Hamann DD, Wu MC. 1985. Development of methods for quality and functionality assesment of surimi and mince fish to be used in gel type food products. Anchorage, AK: Report to Alaska Fisheries Development Foundation, Inc.
    • (1985)
    • Lanier, T.C.1    Hamann, D.D.2    Wu, M.C.3
  • 19
    • 0002834962 scopus 로고
    • Surimi processing technology
    • Lee CM. 1984. Surimi processing technology. Food Technol 38(11):69-80.
    • (1984) Food Technol , vol.38 , Issue.11 , pp. 69-80
    • Lee, C.M.1
  • 20
    • 0001388698 scopus 로고
    • Raman spectroscopy as a probe of protein structure in food systems
    • Yada RY, Jackman RL, Smith JL, editors. London, UK: Blackie Academic and Professional.
    • Li-Chan ECY, Nakai S, Hirotsuka M. 1994. Raman spectroscopy as a probe of protein structure in food systems. In: Yada RY, Jackman RL, Smith JL, editors. Protein structure-function relationsips in foods. London, UK: Blackie Academic and Professional. pp. 163-97.
    • (1994) Protein structure-function relationsips in foods , pp. 163-197
    • Li-Chan, E.C.Y.1    Nakai, S.2    Hirotsuka, M.3
  • 21
    • 79952536911 scopus 로고    scopus 로고
    • Contribution of protein conformation and intermolecular bonds to fish and pork gelation properties
    • Liu RU, Zhao S, Xie B, Xiong S. 2011. Contribution of protein conformation and intermolecular bonds to fish and pork gelation properties. Food Hydrocolloid 25:898-906.
    • (2011) Food Hydrocolloid , vol.25 , pp. 898-906
    • Liu, R.U.1    Zhao, S.2    Xie, B.3    Xiong, S.4
  • 23
    • 33748376956 scopus 로고    scopus 로고
    • Surimi seafood: products, market, and manufacturing
    • Park JW, editor. 2nd ed. Boca Raton, Fla: CRC Press, Taylor & Francis Group, LLC.
    • Park JW. 2005. Surimi seafood: products, market, and manufacturing. In: Park JW, editor. Surimi and surimi seafood. 2nd ed. Boca Raton, Fla: CRC Press, Taylor & Francis Group, LLC. pp. 375-433.
    • (2005) Surimi and surimi seafood , pp. 375-433
    • Park, J.W.1
  • 24
    • 84862780812 scopus 로고    scopus 로고
    • Biochemical characterization of Alaska pollock, Pacific whiting, and threadfin bream surimi as affected by various comminution condition. Submitted to Food Chemistry FOODCHEM-S-12-00306
    • Poowakanjana S, Park JW. 2012. Biochemical characterization of Alaska pollock, Pacific whiting, and threadfin bream surimi as affected by various comminution condition. Submitted to Food Chemistry FOODCHEM-S-12-00306.
    • (2012)
    • Poowakanjana, S.1    Park, J.W.2
  • 25
    • 80053069256 scopus 로고    scopus 로고
    • Thermophysical characterization of tilapia myosin and its subfragments
    • Reed ZH, Park JW. 2011. Thermophysical characterization of tilapia myosin and its subfragments. J Food Sci 76(7):C1050-5.
    • (2011) J Food Sci , vol.76 , Issue.7
    • Reed, Z.H.1    Park, J.W.2
  • 26
    • 77950676908 scopus 로고    scopus 로고
    • Structural changes and dynamic rheological properties of sarcoplasmic proteins subjected to pH-shift method
    • Tadpitchayangkoon P, Park JW, Mayer SG, Yongsawatdigul J. 2010. Structural changes and dynamic rheological properties of sarcoplasmic proteins subjected to pH-shift method. J Agric Food Chem 58:4241-9.
    • (2010) J Agric Food Chem , vol.58 , pp. 4241-4249
    • Tadpitchayangkoon, P.1    Park, J.W.2    Mayer, S.G.3    Yongsawatdigul, J.4
  • 27
    • 33645772484 scopus 로고    scopus 로고
    • Raman spectroscopy determines structural changes associated with gelation properties of fish recovered at alkaline pH
    • Thawornchinsombut S, Park JW, Meng G, Li-Chan ECY. 2006. Raman spectroscopy determines structural changes associated with gelation properties of fish recovered at alkaline pH. J Agric Food Chem 54(6):2178-87.
    • (2006) J Agric Food Chem , vol.54 , Issue.6 , pp. 2178-2187
    • Thawornchinsombut, S.1    Park, J.W.2    Meng, G.3    Li-Chan, E.C.Y.4
  • 28
    • 0036293355 scopus 로고    scopus 로고
    • New structural insights from Raman spectroscopy of proteins and their assemblies
    • Thomas GJ. 2002. New structural insights from Raman spectroscopy of proteins and their assemblies. Biopolymers 67:214-25.
    • (2002) Biopolymers , vol.67 , pp. 214-225
    • Thomas, G.J.1
  • 29
    • 0002660213 scopus 로고
    • Peptide backbone conformation and microenvironment of protein side-chains
    • Clark RJH, Hester RE, editors. New York, USA: John Wiley and Sons.
    • Tu AT. 1986. Peptide backbone conformation and microenvironment of protein side-chains. In: Clark RJH, Hester RE, editors. Spectroscopy of biological systems. New York, USA: John Wiley and Sons. pp. 65-116.
    • (1986) Spectroscopy of biological systems , pp. 65-116
    • Tu, A.T.1
  • 30
    • 0041386023 scopus 로고    scopus 로고
    • Thermal denaturation and aggregation of threadfin bream actomyosin
    • Yongsawatdigul J, Park JW. 2003. Thermal denaturation and aggregation of threadfin bream actomyosin. Food Chem 83:409-16.
    • (2003) Food Chem , vol.83 , pp. 409-416
    • Yongsawatdigul, J.1    Park, J.W.2
  • 31
    • 0036245422 scopus 로고    scopus 로고
    • Slip at polymer-polymer interfaces: rheological measurements on coextruded multilayers
    • Zhao R, Macosko C. 2002. Slip at polymer-polymer interfaces: rheological measurements on coextruded multilayers. J Rheol 46(1):145-67.
    • (2002) J Rheol , vol.46 , Issue.1 , pp. 145-167
    • Zhao, R.1    Macosko, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.