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Volumn 91, Issue 1, 2011, Pages 163-170

Comparative study of in vitro digestibility of major allergen, tropomyosin and other proteins between Grass prawn (Penaeus monodon) and Pacific white shrimp (Litopenaeus vannamei)

Author keywords

Allergen; Digestibility; Grass prawn (Penaeus monodon); Pacific white shrimp (Litopenaeus vannamei); Simulated gastric fluid; Simulated intestinal fluid; Tropomyosin

Indexed keywords

ACTIN; IMMUNOGLOBULIN E; MYOSIN HEAVY CHAIN; PEPSIN A; TROPOMYOSIN;

EID: 78649438355     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.4167     Document Type: Article
Times cited : (50)

References (30)
  • 1
    • 78649437517 scopus 로고    scopus 로고
    • China Fisheries Year Book
    • Anonymous, China Agricultural Press, Beijing
    • Anonymous, China Fisheries Year Book. China Agricultural Press, Beijing (2009).
    • (2009)
  • 2
    • 33751499926 scopus 로고
    • Thermostability and freeze denaturation of Grass prawn (Penaeus monodon) muscle proteins
    • Jiang ST, Hwang BS, Moody MW and Chen HC, Thermostability and freeze denaturation of Grass prawn (Penaeus monodon) muscle proteins. J Agric Food Chem 39: 1998-2001 (1991).
    • (1991) J Agric Food Chem , vol.39 , pp. 1998-2001
    • Jiang, S.T.1    Hwang, B.S.2    Moody, M.W.3    Chen, H.C.4
  • 3
    • 0030529915 scopus 로고    scopus 로고
    • Density-dependent growth and survival of Penaeus setiferus and Penaeus vannamei in a semi-closed recirculating system
    • Williams AS, Davis DA and Arnold CR, Density-dependent growth and survival of Penaeus setiferus and Penaeus vannamei in a semi-closed recirculating system. J World Aquacult Soc 27: 107-112 (1996).
    • (1996) J World Aquacult Soc , vol.27 , pp. 107-112
    • Williams, A.S.1    Davis, D.A.2    Arnold, C.R.3
  • 4
    • 0003432228 scopus 로고    scopus 로고
    • Report of a Joint FAO/WHO Expert Consultation of Allergenicity of Foods Derived from Biotechnology
    • FAO/WHO, in World Health Organization, Geneva
    • FAO/WHO, Evaluation of allergenicity of genetically modified foods, in Report of a Joint FAO/WHO Expert Consultation of Allergenicity of Foods Derived from Biotechnology. World Health Organization, Geneva, pp. 22-25 (2001).
    • (2001) Evaluation of allergenicity of genetically modified foods , pp. 22-25
  • 6
    • 0027386139 scopus 로고
    • Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes
    • Shanti KN, Martin BM, Nagpal S, Metcalfe DD and Rao PV, Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes. J Immunol 151: 5354-5363 (1993).
    • (1993) J Immunol , vol.151 , pp. 5354-5363
    • Shanti, K.N.1    Martin, B.M.2    Nagpal, S.3    Metcalfe, D.D.4    Rao, P.V.5
  • 7
    • 34247846325 scopus 로고    scopus 로고
    • Molecular cloning of tropomyosins identified as allergens in six species of crustaceans
    • Motoyama K, Suma Y, Ishizaki S, Nagashima Y and Shiomi K, Molecular cloning of tropomyosins identified as allergens in six species of crustaceans. J Agric Food Chem 55: 985-991 (2007).
    • (2007) J Agric Food Chem , vol.55 , pp. 985-991
    • Motoyama, K.1    Suma, Y.2    Ishizaki, S.3    Nagashima, Y.4    Shiomi, K.5
  • 8
    • 34147115068 scopus 로고    scopus 로고
    • Comparative analysis of barnacle tropomyosin: divergence from decapod tropomyosins and role as a potential allergen
    • Suma Y, Ishizaki S, Nagashima Y, Lu Y, Ushio H and Shiomi K, Comparative analysis of barnacle tropomyosin: divergence from decapod tropomyosins and role as a potential allergen. Comp Biochem Physiol B Biochem Mol Biol 147: 230-236 (2007).
    • (2007) Comp Biochem Physiol B Biochem Mol Biol , vol.147 , pp. 230-236
    • Suma, Y.1    Ishizaki, S.2    Nagashima, Y.3    Lu, Y.4    Ushio, H.5    Shiomi, K.6
  • 9
    • 0028104397 scopus 로고
    • Cloning, expression, and primary structure of Metapenaeus ensis tropomyosin, the major heat-stable shrimp allergen
    • Leung PSC, Chu KH, Chow WK, Ansari A, Bandea CI, Kwan HS, et al, Cloning, expression, and primary structure of Metapenaeus ensis tropomyosin, the major heat-stable shrimp allergen. J Allergy Clin Immunol 94: 882-890 (1994).
    • (1994) J Allergy Clin Immunol , vol.94 , pp. 882-890
    • Leung, P.S.C.1    Chu, K.H.2    Chow, W.K.3    Ansari, A.4    Bandea, C.I.5    Kwan, H.S.6
  • 10
    • 46949104405 scopus 로고    scopus 로고
    • Identification and characterization of the major allergen of Chinese mitten crab (Eriocheir sinensis)
    • Liang YL, Cao MJ, Su WJ, Zhang LJ, Huang YY and Liu GM, Identification and characterization of the major allergen of Chinese mitten crab (Eriocheir sinensis). Food Chem 111: 998-1003 (2008).
    • (2008) Food Chem , vol.111 , pp. 998-1003
    • Liang, Y.L.1    Cao, M.J.2    Su, W.J.3    Zhang, L.J.4    Huang, Y.Y.5    Liu, G.M.6
  • 11
    • 74249119824 scopus 로고    scopus 로고
    • Effects of boiling on the allergenic properties of tropomyosin of shrimp (Litopenaeus vannamei)
    • Liu GM, Cheng H, Nesbit JB, Su WJ, Cao MJ and Maleki SJ, Effects of boiling on the allergenic properties of tropomyosin of shrimp (Litopenaeus vannamei). J Food Sci 75: T1-T5 (2010).
    • (2010) J Food Sci , vol.75
    • Liu, G.M.1    Cheng, H.2    Nesbit, J.B.3    Su, W.J.4    Cao, M.J.5    Maleki, S.J.6
  • 12
    • 0029853999 scopus 로고    scopus 로고
    • IgE reactivity against a cross-reactive allergen in crustacea and mollusca: Evidence for tropomyosin as the common allergen
    • Leung PSC, Chow WK, Duffey S, Kwan HS, Gershwin ME and Chu KH, IgE reactivity against a cross-reactive allergen in crustacea and mollusca: Evidence for tropomyosin as the common allergen. J Allergy Clin Immunol 98: 954-961 (1996).
    • (1996) J Allergy Clin Immunol , vol.98 , pp. 954-961
    • Leung, P.S.C.1    Chow, W.K.2    Duffey, S.3    Kwan, H.S.4    Gershwin, M.E.5    Chu, K.H.6
  • 13
    • 69149106437 scopus 로고    scopus 로고
    • In vitro digestion methods for assessing the effect of food structure on allergen breakdown
    • Wickham M, Faulks R and Mills C, In vitro digestion methods for assessing the effect of food structure on allergen breakdown. Mol Nutr Food Res 53: 952-958 (2009).
    • (2009) Mol Nutr Food Res , vol.53 , pp. 952-958
    • Wickham, M.1    Faulks, R.2    Mills, C.3
  • 14
    • 0029764078 scopus 로고    scopus 로고
    • Stability of food allergens to digestion in vitro
    • Astwood JD, Leach JN and Fuchs RL, Stability of food allergens to digestion in vitro. Nat Biotechnol 14: 1269-1273 (1996).
    • (1996) Nat Biotechnol , vol.14 , pp. 1269-1273
    • Astwood, J.D.1    Leach, J.N.2    Fuchs, R.L.3
  • 15
    • 0037145909 scopus 로고    scopus 로고
    • Digestibility of food allergens and nonallergenic proteins in simulated gastric fluid and simulated intestinal fluid-A comparative study
    • Fu TJ, Abbott UR and Hatzos C, Digestibility of food allergens and nonallergenic proteins in simulated gastric fluid and simulated intestinal fluid-A comparative study. J Agric Food Chem 50: 7154-7160 (2002).
    • (2002) J Agric Food Chem , vol.50 , pp. 7154-7160
    • Fu, T.J.1    Abbott, U.R.2    Hatzos, C.3
  • 16
    • 55449094462 scopus 로고    scopus 로고
    • Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein
    • Bublin M, Radauer C, Knulst A, Wagner S, Scheiner O, Mackie AR, et al, Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein. Mol Nutr Food Res 52: 1130-1139 (2008).
    • (2008) Mol Nutr Food Res , vol.52 , pp. 1130-1139
    • Bublin, M.1    Radauer, C.2    Knulst, A.3    Wagner, S.4    Scheiner, O.5    Mackie, A.R.6
  • 17
    • 61349161803 scopus 로고    scopus 로고
    • Should digestion assays be used to estimate persistence of potential allergens in tests for safety of novel food proteins?
    • Schnell S and Herman RA, Should digestion assays be used to estimate persistence of potential allergens in tests for safety of novel food proteins? Clin Mol Allergy 7: 1-7 (2009).
    • (2009) Clin Mol Allergy , vol.7 , pp. 1-7
    • Schnell, S.1    Herman, R.A.2
  • 18
    • 33847136084 scopus 로고    scopus 로고
    • Purification and characterization of sea bream (Sparus latus Houttuyn) pepsinogens and pepsins
    • Zhou Q, Fu XP, Zhang LJ, Su WJ and Cao MJ, Purification and characterization of sea bream (Sparus latus Houttuyn) pepsinogens and pepsins. Food Chem 103: 795-801 (2007).
    • (2007) Food Chem , vol.103 , pp. 795-801
    • Zhou, Q.1    Fu, X.P.2    Zhang, L.J.3    Su, W.J.4    Cao, M.J.5
  • 19
    • 11844283395 scopus 로고    scopus 로고
    • Identification of a myofibril-bound serine proteinase in the skeletal muscle of silver carp
    • Cao MJ, Shao W, Li Y, Hara K, Wang XC and Su WJ, Identification of a myofibril-bound serine proteinase in the skeletal muscle of silver carp. J Food Biochem 28: 373-386 (2004).
    • (2004) J Food Biochem , vol.28 , pp. 373-386
    • Cao, M.J.1    Shao, W.2    Li, Y.3    Hara, K.4    Wang, X.C.5    Su, W.J.6
  • 20
    • 22144478600 scopus 로고    scopus 로고
    • Fish fast skeletal muscle tropomyosins show species-specific thermal stability
    • Huang MC and Ochiai Y, Fish fast skeletal muscle tropomyosins show species-specific thermal stability. Comp Biochem Physiol B Biochem Mol Biol 141: 461-471 (2005).
    • (2005) Comp Biochem Physiol B Biochem Mol Biol , vol.141 , pp. 461-471
    • Huang, M.C.1    Ochiai, Y.2
  • 22
    • 84905247515 scopus 로고
    • The United States Pharmacopeia 23
    • US Pharmacopoeia, the National Formulary., in, The National Formulary 18, The United States Pharmacopeial Convention Inc., Rockville, MD
    • US Pharmacopoeia, the National Formulary. Simulated gastric fluid and simulated intestinal fluid, TS, in The United States Pharmacopeia 23, The National Formulary 18, The United States Pharmacopeial Convention Inc., Rockville, MD, p. 2053 (1995).
    • (1995) Simulated gastric fluid and simulated intestinal fluid, TS , pp. 2053
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli UK, Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227: 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T and Gordon J, Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci U S A 76: 4350-4354 (1979).
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 25
    • 33846149646 scopus 로고    scopus 로고
    • Changes in allergenicity and digestibility of squid tropomyosin during the maillard reaction with ribose
    • Nakamura A, Sasaki F, Watanabe K, Ojima T, Ahn DH and Saeki H, Changes in allergenicity and digestibility of squid tropomyosin during the maillard reaction with ribose. J Agric Food Chem 54: 9529-9534 (2006).
    • (2006) J Agric Food Chem , vol.54 , pp. 9529-9534
    • Nakamura, A.1    Sasaki, F.2    Watanabe, K.3    Ojima, T.4    Ahn, D.H.5    Saeki, H.6
  • 26
    • 84944052122 scopus 로고    scopus 로고
    • Handbook of Proteolytic Enzymes
    • 2nd edition. Elsevier, London
    • Barrett AJ, Rawlings ND and Woessner JF, Handbook of Proteolytic Enzymes, 2nd edition. Elsevier, London (2004).
    • (2004)
    • Barrett, A.J.1    Rawlings, N.D.2    Woessner, J.F.3
  • 27
    • 0036266609 scopus 로고    scopus 로고
    • Digestion stability as a criterion for protein allergenicity assessment
    • Fu TJ, Digestion stability as a criterion for protein allergenicity assessment. Ann NY Acad Sci 964: 99-110 (2002).
    • (2002) Ann NY Acad Sci , vol.964 , pp. 99-110
    • Fu, T.J.1
  • 28
    • 33846567968 scopus 로고    scopus 로고
    • Gastrointestinal digestion of food allergens: effect on their allergenicity
    • Moreno FJ, Gastrointestinal digestion of food allergens: effect on their allergenicity. Biomed Pharmacother 61: 50-60 (2007).
    • (2007) Biomed Pharmacother , vol.61 , pp. 50-60
    • Moreno, F.J.1
  • 30
    • 10044298125 scopus 로고    scopus 로고
    • Allergenicity of crustacean extractives and its reduction by protease digestion
    • Shimakura K, Tonomura Y, Hamada Y, Nagashima Y and Shiomi K, Allergenicity of crustacean extractives and its reduction by protease digestion. Food Chem 91: 247-253 (2005).
    • (2005) Food Chem , vol.91 , pp. 247-253
    • Shimakura, K.1    Tonomura, Y.2    Hamada, Y.3    Nagashima, Y.4    Shiomi, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.