Abstract
Stock depletion, new trends in farming practices, the globalization of markets, and the development of novel products and production methods represent new challenges for seafood quality and safety. Fortunately, genomics, proteomics, and high-throughput microarray technologies have fundamentally changed our ability to study the molecular basis of aspects related to food authenticity, safety, and quality as well as changes induced by processing in food matrices. Furthermore, knowledge about the localization, structure, modification, function, and interactions of the proteins expressed by a genome from any tissue used as a source of food can offer precious information in order to improve its quality, safety, and nutritional properties. Although fish protein databases are still scarce, especially when compared with those available for edible plants and terrestrial animals, proteomics studies of model aquatic organisms are helping us to understand problems related to the quality and safety of seafood. The main objective of this chapter is to present a compilation of studies related to fish quality aspects by means of proteomics tools describing new perspectives and challenges for the use of proteomics-based biomarkers in the identification of the causes of quality flaws and their prevention.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Abee T, Van Schaik W, Siezen RJ (2004) Impact of genomics on microbial food safety. Trends Biotechnol 22:653ā660
Addis MF, Cappuccinelli R, Tedde V, Pagnozzi D, Porcu MC, Bonaglini E, Roggio T, Uzzau S (2010) Proteomic analysis of muscle tissue from gilthead sea bream (Sparus aurata L.) farmed in offshore floating cages. Aquaculture 309(1):245ā252
Bauchart C, Chambon C, Mirand PP, Savary-Auzeloux I, RĆ©mond D, Morzel M (2007) Peptides in rainbow trout (Oncorhynchus mykiss) muscle subjected to ice storage and cooking. Food Chem 100:1566ā1572
Bendixen E, Danielsen M, Hollung K, Gianazza E, Miller I (2011) Farm animal proteomics ā a review. J Proteomics 74:282ā293
BiĆØche C, de Lamballerie M, Chevret D, Federighi M, Tresse O (2011) Dynamic proteome changes in Campylobacter jejuni 81-176 after high pressure shock and subsequent recovery. Ann NY Acad Sci 1189:133ā138
Bƶhme K, FernĆ”ndez-No IC, Barros-VelĆ”zquez J, Gallardo JM, CaƱas B, Calo-Mata P (2010a) Comparative analysis of protein extraction methods for the identification of seafood-borne pathogenic and spoilage bacteria by MALDI-TOF mass spectrometry. Anal Method 2:1941ā1947
Bƶhme K, FernĆ”ndez-No IC, Barros-VelĆ”zquez J, Gallardo JM, Calo-Mata P, CaƱas B (2010b) Species differentiation of seafood spoilage and pathogenic Gram-negative bacteria by MALDI-TOF mass fingerprinting. J Proteome Res 9:3169ā3183
Bƶhme K, FernĆ”ndez-No IC, Barros-VelĆ”zquez J, Gallardo JM, CaƱas B, Calo-Mata P (2011a) Rapid species identification of seafood spoilage and pathogenic Gram-positive bacteria by MALDI-TOF mass fingerprinting. Electrophoresis 32:2951ā2965
Bƶhme K, FernĆ”ndez-No IC, Gallardo JM, CaƱas B, Calo-Mata P (2011b) Safety assessment of fresh and processed seafood products by MALDI-TOF mass fingerprinting. Food Bioprocess Technol 4:907ā918
Bohne-Kjersem A, Skadsheim A, GoksĆøyr A, GrĆøsvik BE (2009) Candidate biomarker discovery in plasma of juvenile cod (Gadus morhua) exposed to crude North Sea oil, alkyl phenols and polycyclic aromatic hydrocarbons (PAHs). Mar Environ Res 68:268ā277
Bohne-Kjersem A, Bache N, Meier S, Nyhammer G, Roepstorff P, SƦle Ć, GoksĆøyr A, GrĆøsvik BE (2010) Biomarker candidate discovery in Atlantic cod Gadus morhua continuously exposed to North Sea produced water from egg to fry. Aquat Toxicol 96:280ā289
BorderĆas AJ, SĆ”nchez-Alonso I (2011) First processing steps and the quality of wild and farmed fish. J Food Sci 76:1ā5
Cacace G, Mazzeo MF, Sorrentino A, Spada V, Malorni A, Siciliano RA (2010) Proteomics for the elucidation of cold adaptation mechanisms in Listeria monocytogenes. J Proteomics 73:2021ā2030
Cifuentes A, Dugo P, Fanali S (2011) Advances in food analysis. J Chromatogr A 1218:7385
Dory D, Chopin C, Aimone-Gasti I, Gueant JL, Sainte-Laudy J, Moneret-Vautrin DA, Fleurence J (1998) Recognition of an extensive range of IgE-reactive proteins in cod extract. Allergy 53:42ā50
Eriksson J, Fenyƶ D (2005) Protein identification in complex mixtures. J Proteome Res 4:387ā393
FAO (2005) Fisheries and aquaculture topics. Quality of fish and fish products. Topics fact sheets. Text by Lahsen Ababouch. In: FAO fisheries and aquaculture department [online]. Rome. Updated 27 May 2005
FernĆ”ndez-No IC, Bƶhme K, Calo-Mata P, Barros-VelĆ”zquez J (2011) Characterisation of histamine-producing bacteria from farmed blackspot seabream Pagellus bogaraveo and turbot Psetta maxima. Int J Food Microbiol 151:182ā189
FernĆ”ndez-No IC, Bƶhme K, Calo-Mata P, CaƱas B, Gallardo JM, Barros-VelĆ”zquez J (2012) Isolation and characterization of Streptococcus parauberis from vacuum-packaging refrigerated seafood products. Food Microbiol 30:91ā97
FornĆ© I, AbiĆ”n J, CerdĆ J (2010) Fish proteome analysis: model organisms and non-sequenced species. Proteomics 10:858ā872
Gebriel M, Uleberg K, Larssen E, Hjelle BjĆørnstad A, Sivertsvik M, MĆøller SG (2010) Cod (Gadus morhua) muscle proteome cataloging using 1D-PAGE protein separation, nano-liquid chromatography peptide fractionation and linear trap quadrupole LTQ mass spectrometry. J Agric Food Chem 58:12307ā12312
Ghaly AE, Dave D, Budge S, Brooks MS (2010) Fish spoilage mechanisms and preservation techniques: review. Am J Appl Sci 7:846ā864
Graham DRM, Elliott ST, Van Eyk JE (2005) Broad-based proteomic strategies: a practical guide to proteomics and functional screening. J Physiol 563:1ā9
Gram L, Huss HH (2000) Fresh and processed fish and shellfish. In: Lund BM, Baird-Parker AC, Gould GW (eds) The microbiological safety and quality of foods. Chapman and Hall, London, pp 472ā506
Grunert KG (2005) Food quality and safety: consumer perception and demand. Eur Rev Agric Econ 32:369ā391
GudmundsdĆ³ttir S, Roche SM, Kristinsson K, KristjĆ”nsson M (2006) Virulence of Listeria monocytogenes isolates from humans and smoked salmon, peeled shrimp and their processing environments. J Food Prot 69:2157ā2160
Guilbaud M, Chafsey I, Pilet M, Leroi F, PrĆ©vost H, HĆ©braud M, Dousset X (2008) Response of Listeria monocytogenes to liquid smoke. J Appl Microbiol 104:1744ā1753
Havelaar AH, Brul S, de Jong A, de Jonge R, Zwietering MH, Ter Kuile BH (2010) Future challenges to microbial food safety. Int J Food Microbiol 139:S79āS94
Hazen TH, Martinez RJ, Chen Y, Lafon PC, Garrett NM, Parsons MB, Sobecky PA (2009) Rapid identification of Vibrio parahaemolyticus by whole-cell matrix-assisted laser desorption ionization-time of flight mass spectrometry. Appl Environ Microbiol 75:6745ā6756
Herrero M, SimƵ C, GarcĆa-CaƱas V, IbƔƱez E, Cifuentes A (2012) Foodomics: MS-based strategies in modern food science and nutrition. Mass Spectrom Rev 31:49ā69
Hocquette J, Richardson RI, Prache S, Medale F, Duffy G, Scollan ND (2005) The future trends for research on quality and safety of animal products. Ital J Anim Sci 4:49ā72
Hogstrand C, Balesaria S, Glover CN (2002) Application of genomics and proteomics for study of the integrated response to zinc exposure in a non-model fish species, the rainbow trout. Comp Biochem Physiol 133B:523ā535
Ishida T, Ishii Y, Yamada H, Oguri K (2002) The induction of hepatic selenium-binding protein by aryl hydrocarbon (Ah)-receptor ligands in rats. J Health Sci 48:62ā68
Kinoshita Y, Sato T, Naitou H, Ohashi N, Kumazawa S (2007) Proteomic studies on protein oxidation in bonito (Katsuwonus pelamis) muscle. Food Sci Technol Res 13:133ā138
KjƦrsgĆ„rd IVH, Jessen F (2003) Proteome analysis elucidating post-mortem changes in cod (Gadus morhua) muscle proteins. J Agric Food Chem 51:3985ā3991
KjƦrsgƄrd IVH, Jessen F (2004) Oxidation of protein in rainbow trout muscle. In: Proceedings of the 34th WEFTA conference. 184. http://www.wefta.org
KjƦrsgĆ„rd IVH, NĆørrelykke MR, Jessen F (2006a) Changes in cod muscle proteins during frozen storage revealed by proteome analysis and multivariate data analysis. Proteomics 6:1606ā1618
KjƦrsgĆ„rd IVH, NĆørrelykke MR, Baron CP, Jessen F (2006b) Identification of carbonylated protein in frozen rainbow trout (Oncorhynchus mykiss) fillets and development of protein oxidation during frozen storage. J Agric Food Chem 54:9437ā9446
Lu J, Zheng J, Liu H, Li J, Chen H, Chen K (2010) Protein profiling analysis of skeletal muscle of a pufferfish, Takifugu rubripes. Mol Biol Rep 37:2141ā2147
Malik AK, Blasco C, PicĆ³ Y (2010) Liquid chromatography-mass spectrometry in food safety. J Chromatogr A 1217:4018ā4040
Martin SAM, Vilhelmsson O, MĆ©dale F, Watt P, Kaushik S, Houlihan DB (2003) Proteomic sensitivity to dietary manipulations in rainbow trout. BBA 1651:17ā29
Martinez I (1992) Fish myosin degradation upon storage. In: Huss HH, Jakobsen M, Liston J (eds) Quality assurance in the fish industry. Elsevier Science, Amsterdam, pp 389ā397
Martinez I, Ofstad R, Olsen RL (1990) Myosin isoforms in red and white muscles of some teleost fishes. J Muscle Res Cell Motil 11:489ā495
Martinez I, Christiansen JS, Ofstad R, Olsen RL (1991) Comparison of myosin isoenzymes present in skeletal and cardiac muscles of the Arctic charr Salvelinus alpinus (L.). Sequential expression of different myosin heavy chains during development of the fast white skeletal muscle. Eur J Biochem 195:743ā753
Martinez I, Solberg C, Lauritzen K, Ofstad R (1992) Two-dimensional electrophoretic analyses of cod (Gadus morhua, L.) whole muscle proteins, water-soluble fraction and surimi. Effect of the addition of CaCl2 and MgCl2 during the washing procedure. Appl Theor Electrophor 2:201ā206
Martinez I, Slizyte R, Dauksas E (2007) High resolution two-dimensional electrophoresis as a tool to differentiate wild from farmed cod (Gadus morhua) and to assess the protein composition of klipfish. Food Chem 101:1337ā1343
Meier S, Morton HC, Nyhammer G, GrĆøsvik BE, Makhotin V, Geffen A, Boitsov S, Kvestad KA, Bohne-Kjersem A, GoksĆøyr A, Folkvord A, KlungsĆøyr J, Svardal A (2010) Development of Atlantic cod (Gadus morhua) exposed to produced water during early life stages: effects on embryos, larvae and juvenile fish. Mar Environ Res 70:383ā394
Miracle AL, Ankley GT (2005) Ecotoxicogenomics: linkages between exposure and effects in assessing risks of aquatic contaminants to fish. Reprod Toxicol 19:321ā326
Monti G, De Napoli L, Mainolfi P, Barone R, Guida M, Marino G, Amoresano A (2005) Monitoring food quality by microfluidic electrophoresis, gas chromatography and mass spectrometry techniques: effects of aquaculture on the sea bass (Dicentrarchus labrax). Anal Chem 77:2587ā2594
Morzel M, Verrez-Bagnis V, Arendt EK, Fleurence J (2000) Use of two-dimensional electrophoresis to evaluate proteolysis in salmon (Salmo salar) muscle as affected by a lactic fermentation. J Agric Food Chem 48:239ā244
Morzel M, Chambon C, LefĆØvre F, Paboeuf G, Laville E (2006) Modifications of trout (Oncorhynchus mykiss) muscle proteins by preslaughter activity. J Agric Food Chem 54:2997ā3001
Nini H, Sissener NH, Martin SAM, Cash P, HevrĆøy EM, Sanden M, Hemre GI (2010) Proteomic profiling of liver from Atlantic salmon (Salmo salar) fed genetically modified soy compared to the near-isogenic non-GM line. Mar Biotechnol 12:273ā281
Norton DM, Scarlett JM, Horton K, Sue D, Thimothe J, Boor KJ, Wiedmann M (2001) Characterization and pathogenic potential of Listeria monocytogenes isolates from the smoked fish industry. Appl Environ Microbiol 67:646ā653
OāFlaherty S, Klaenhammer TR (2011) The impact of omic technologies on the study of food microbes. Ann Rev Food Sci Technol 2:353ā371
Ochiai Y (2010) Changes in quality and denaturation of sarcoplasmic protein components in the burnt meat of bluefin tuna (Thunnus thynnus orientalis). Nippon Suisan Gakkaishi Jpn Ed 76:695ā704
Ochiai Y, Kobayashi T, Watabe S, Hashimoto K (1990) Mapping of fish myosin light chains by two-dimensional gel electrophoresis. Comp Biochem Physiol 95B:341ā345
Pazos M, Da Rocha AP, Roepstorff P, Rogowska-Wrzesinska A (2011) Fish proteins as targets of ferrous-catalyzed oxidation: identification of protein carbonyls by fluorescent labelling on two-dimensional gels and MALDI-TOF/TOF mass spectrometry. J Agric Food Chem 59:7962ā7977
Pedreschi R, Maarten H, Lilley KS, Bart N (2010) Proteomics for the food industry: opportunities and challenges. CRC Crit Rev Food Sci Nutr 50:680ā692
PiƱeiro C, VelĆ”zquez JB, Sotelo CG, PĆ©rez-MartĆn RI, Gallardo JM (1998) Two-dimensional electrophoretic study of the water-soluble protein fraction in white muscle of Gadoid fish species. J Agric Food Chem 46:3991ā3997
PiƱeiro C, VĆ”zquez J, Marina AI, Barros-VelĆ”zquez J, Gallardo JM (2001) Characterization and partial sequencing of species-specific sarcoplasmic polypeptides from commercial hake species by mass spectrometry following 2-DE analysis. Electrophoresis 22:1545ā1552
PiƱeiro C, Barros-VelĆ”zquez J, VĆ”zquez J, Figueras A, Gallardo JM (2003) Proteomics as a tool for the investigation of seafood and other marine products. J Proteome Res 2:127ā135
PiƱeiro C, CaƱas B, Carrera M (2010) The role of proteomics in the study of the influence of climate change on seafood products. Food Res Int 43:1791ā1802
Pinstrup-Andersen P (2009) Food security. Definition and measurement. Food Secur 1:5ā7
Pischetsrieder M, Baeuerlein R (2009) Proteome research in food science. Chem Soc Rev 38:2600ā2608
Prunet P, Ćverli Ć, Douxfils J, Bernardini G, Kestemont P, Baron C (2012) Fish welfare and genomics. Fish Physiol Biochem 38:43ā60
Roth B, GrimsbĆø E, Slinde E, Foss A, Stien LH, Nortvedt R (2012) Crowding, pumping and stunning of Atlantic salmon, the subsequent effect on pH and rigor mortis. Aquaculture 326ā329:178ā180
Sanchez-Dardon J, Voccia I, Hontela A, Chilmonczyk S, Dunier M, Boermans H, Blakley B, Fournier M (1999) Immunomodulation by heavy metals tested individually or in mixtures in rainbow trout (Oncorhynchus mykiss) exposed in vivo. Environ Toxicol Chem 18:1492ā1497
Santesmases M (2004) Marketing. Conceptos y Estrategias. Edit. PirƔmide, S.A. Madrid. 1120 pp
Schiavone R, Zilli L, Storelli C, Vilella S (2008) Identification by proteome analysis of muscle proteins in sea bream (Sparus aurata). Eur Food Res Technol 227:1403ā1410
Self RL, Wu W, Marks HS (2011) Simultaneous quantification of eight biogenic amine compounds in tuna by matrix solid-phase dispersion followed by HPLC-orbitrap mass spectrometry. J Agric Food Chem 59:5906ā5913
Terlouw EMC, Arnould C, Auperin B, Berri C, Le Bihan-Duval E, Deiss V et al (2008) Pre-slaughter conditions, animal stress and welfare: current status and possible future research. Animal 2:1501ā1517
Terova G, Addis MF, Preziosa E, Pisanu S, Pagnozzi D, Biosa G, Gomati R, Bernadini G, Roggio T, Saroglia M (2011) Effects of post mortem storage temperature on sea bass (Dicentrarchus labrax) muscle protein degradation: analysis by 2-D DIGE and MS. Proteomics 11:2901ā2910
Van Vliet E (2011) Current standing and future prospects for the technologies proposed to transform toxicity testing in the 21st century. ALTEX 28:17ā44
Veiseth-Kent E, Grove H, FƦrgestad EM, FjƦra SO (2010) Changes in muscle and blood plasma proteomes of Atlantic salmon (Salmo salar) induced by crowding. Aquaculture 309:272ā279
VerdĆŗ AJ (2003) Una escala multi-Ćtem para la mediciĆ³n de la calidad percibida en alimentos y bebidas. Rev Eur DirecciĆ³n y Econ Empresa 12:59ā76
Verrez-Bagnis V, Ladrat C, Morzel M, NoĆ«l J, Fleurence J (2001) Protein changes in post mortem sea bass (Dicentrarchus labrax) muscle monitored by one- and two-dimensional gel electrophoresis. Electrophoresis 22:1539ā1544
Videler J (2011) An opinion paper: emphasis on white muscle development and growth to improve farmed fish flesh quality. Fish Physiol Biochem 37:337ā343
Wang PA, Vang B, Pedersen AM, Martinez I, Olsen RL (2011) Post-mortem degradation of myosin heavy chain in intact fish muscle: effects of pH and enzyme inhibitors. Food Chem 124:1090ā1095
Watabe S, Hwang GC, Nakaya M, Guo XF, Okamoto Y (1992) Fast skeletal myosin isoforms in thermally acclimated carp. J Biochem 111:113ā122
Welker M (2011) Proteomics for routine identification of microorganisms. Proteomics 11:3143ā3153
Yaktine AL, Nesheim MC, James CA (2008) Nutrient and contaminant tradeoffs: exchanging meat, poultry, or seafood for dietary protein. Nutr Rev 66:113ā122
Yamashita M (2010) Stress responses of fish during catching process. In: Konno K, Ochia Y, Fukuda Y (eds) Quality control of tuna meat by optimization of fishing and handling. Koseisha-Koseikaku, Tokyo, pp 81ā94
Yamashita Y, Yamashita M (2010) Identification of a novel selenium-containing compound, selenoneine, as the predominant chemical form of organic selenium in the blood of bluefin tuna. J Biol Chem 285:18134ā18138
Yamashita Y, Yabu T, Yamashita M (2010) Discovery of the strong antioxidant selenoneine in tuna and selenium redox metabolism. World J Biol Chem 1:144ā150
Zhang XW, Yap Y, Wei D, Chen G, Chen F (2008) Novel omics technologies in nutrition research. Biotechnol Adv 26:169ā176
Zhu JY, Huang HQ, Bao XD, Lin QM, Cai ZW (2006) Acute toxicity profile of cadmium revealed by proteomics in brain tissue of Paralichthys olivaceus: potential role of transferrin in cadmium toxicity. Aquat Toxicol 78:127ā135
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
Ā© 2013 Springer Science+Business Media New York
About this chapter
Cite this chapter
PiƱeiro, C., Martinez, I. (2013). Evaluation of Fish Quality and Safety by Proteomics Techniques. In: ToldrƔ, F., Nollet, L. (eds) Proteomics in Foods. Food Microbiology and Food Safety, vol 2. Springer, Boston, MA. https://doi.org/10.1007/978-1-4614-5626-1_10
Download citation
DOI: https://doi.org/10.1007/978-1-4614-5626-1_10
Published:
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4614-5625-4
Online ISBN: 978-1-4614-5626-1
eBook Packages: Chemistry and Materials ScienceChemistry and Material Science (R0)