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Effect of pH on the physicochemical and heat-induced gel properties of scallop Patinopecten yessoensis actomyosin

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  • Food Science and Technology
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Abstract

Gelation is an important functional property of protein in meats. In this study, we prepared actomyosin from scallop Patinopecten yessoensis adductor muscles and studied the effects of pH on the physicochemical properties of the actomyosin preparation and on its heat-induced gel-forming properties. The results showed that the turbidity and surface hydrophobicity of scallop actomyosin increased with increases in the heating temperature, while the α-helical content concomitantly decreased. Higher turbidity and surface hydrophobicity and lower α-helical content were found to be easily obtained at lower pH values. A high water-holding capacity, strong gel strength, fine gel network and uniform ice crystals were all clearly observed at pH 7.0, indicating that a neutral pH was most beneficial for formation of the heat-induced scallop actomyosin gel. We therefore conclude that both the physicochemical properties of scallop actomyosin and its gel-forming ability during the heating process are pH dependent.

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References

  1. Wang H, Pato M, Pietrasik Z, Shand P (2009) Biochemical and physicochemical properties of thermally treated natural actomyosin extracted from normal and PSE pork Longissimus muscle. Food Chem 113:21–27

    Article  CAS  Google Scholar 

  2. Lanier TC, Carvajal P, Yongsawatdigul J (2005) Surimi gelation chemistry. In: Park JW (ed) Surimi and surimi seafood, 2nd edn. CRC Press, Florida, pp 436–489

  3. Lefevre F, Fauconneau B, Ouali A, Culioli J (2002) Thermal gelation of brown trout myofibrils from white and red muscle: effect of pH and ionic strength. J Sci Food Agric 82:452–463

    Article  CAS  Google Scholar 

  4. Feng Y, Hultin HO (2001) Effect of pH on the rheological and structural properties of gels of water-washed chicken-breast muscle at physiological ionic strength. J Agric Food Chem 49:3927–3935

    Article  PubMed  CAS  Google Scholar 

  5. Hayashi K, Azuma Y, Koseki S, Konno K (2007) Different effects of ionic and non-ionic compounds on the freeze denaturation of myofibrils and myosin subfragment-1. Fish Sci 73:178–183

    Article  CAS  Google Scholar 

  6. Takahashi M, Yamanoto T, Kato S, Konno K (2005) Species-specific thermal denaturation pattern of fish myosin when heated as myofibrils as studied by myosin subfragment-1 and rod denaturation rater. Fish Sci 71:405–413

    Article  CAS  Google Scholar 

  7. Tao Y, Kobayashi M, Fukushima H, Watabe S (2005) Changes in enzymatic and structural properties of grass carp fast skeletal myosin induced by the laboratory-conditioned thermal acclimation and seasonal acclimatization. Fish Sci 71:195–204

    Article  CAS  Google Scholar 

  8. Liu R, Zhao SM, Xiong SB, Xie BJ, Qin LH (2008) Role of secondary structures in the gelation of porcine myosin at different pH values. Meat Sci 80:632–639

    Article  PubMed  CAS  Google Scholar 

  9. Liu R, Zhao SM, Xiong SB, Qiu CG, Xie BJ (2008) Rheological properties of fish actomyosin and pork actomyosin solutions. J Food Eng 85:173–179

    Article  CAS  Google Scholar 

  10. Raghavan S, Kristinsson HG (2008) Conformational and rheological changes in catfish myosin during alkali-induced unfolding and refolding. Food Chem 107:385–398

    Article  CAS  Google Scholar 

  11. Westphalen AD, Briggs JL, Lonergan SM (2005) Influence of pH on rheological properties of porcine myofibrillar protein during heat induced gelation. Meat Sci 70:293–299

    Article  PubMed  CAS  Google Scholar 

  12. Riebroy S, Benjakul S, Visessanguan W, Tanaka M (2007) Changes during fermentation of Som-fug produced from different marine fish. J Food Process Pres 31:751–770

    Article  CAS  Google Scholar 

  13. Kristinsson HG, Liang Y (2006) Effect of pH-shift processing and surimi processing on Atlantic croaker (Micropogonias undulates) muscle proteins. J Food Sci 71:C304–C312

    Article  CAS  Google Scholar 

  14. Pérez-Mateos M, Lanier TC (2007) Comparison of Atlantic menhaden gels from surimi processed by acid or alkaline solubilization. Food Chem 101:1223–1229

    Article  Google Scholar 

  15. Kristinsson HG, Hultin HO (2003) Effect of low and high pH treatment on the functional properties of cod muscle proteins. J Agric Food Chem 51:5103–5110

    Article  PubMed  CAS  Google Scholar 

  16. Kristinsson HG, Hultin HO (2003) Changes in conformation and subunit assembly of cod myosin at low and high pH and after subsequent refolding. J Agric Food Chem 51:7187–7196

    Article  PubMed  CAS  Google Scholar 

  17. Pérez-Mateos M, Amato PM, Lanier TC (2004) Gelling properties of Atlantic croaker surimi processed by acid or alkaline solubilization. J Food Sci 69:328–333

    Google Scholar 

  18. Karayannakidis PD, Zotos A, Petridis D, Taylor KDA (2007) The effect of initial wash at acidic and alkaline pHs on the properties of protein concentrate (kamaboko) products from sardine (Sardina pilchardus) samples. J Food Eng 78:775–783

    Article  CAS  Google Scholar 

  19. Campo-Deaño L, Tovar CA, Pombo MJ, Solas MT, Borderías AJ (2009) Rheological study of giant squid surimi (Dosidicus gigas) made by two methods with different cryoprotectants added. J Food Eng 94:26–33

    Article  Google Scholar 

  20. Paredi ME, De Vido de Mattio N, Crupkin M (1990) Biochemical properties of actomyosin of cold stored striated adductor muscles of Aulacomya ater ater (Molina). J Food Sci 55:1567–1570

    Article  CAS  Google Scholar 

  21. Benjakul S, Visessanguan W, Ishizaki S, Tanaka M (2001) Differences in gelation characteristics of natural actomyosin from two species of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus. J Food Sci 66:1311–1318

    Article  CAS  Google Scholar 

  22. Wang H, Pato MD, Shand PJ (2005) Biochemical properties of natural actomyosin extracted from normal and pale, soft, and exudative pork loin after frozen storage. J Food Sci 70:313–320

    Article  Google Scholar 

  23. Kocher PN, Foegeding EA (1993) Microcentrifuge-based method for measuring water-holding of protein gels. J Food Sci 58:1040–1046

    Article  CAS  Google Scholar 

  24. Giménez B, Gómez-Guillén M, Montero P (2005) Storage of dried fish on quality characteristics of extracted gelatin. Food Hydrocolloid 19:958–963

    Article  Google Scholar 

  25. Laemmliu K (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685

    Article  Google Scholar 

  26. Liu R, Zhao SM, Liu YM, Yang H, Xiong SB, Xie BJ, Qin LH (2010) Effect of pH on the gel properties and secondary structure of fish myosin. Food Chem 121:196–202

    Article  CAS  Google Scholar 

  27. Jiang HM, Dong XP, Wang JT, Zhu BW (2009) Turbidity and viscosity properties of myofibril from scallop. Food Machinery (in Chinese edition) 25:18–21

    Google Scholar 

  28. Li-Chan E, Nakai S, Wood DF (1985) Relationship between functional (fat binding, emulsifying) and physicochemical properties of muscle proteins: effects of heating, freezing, pH and species. J Food Sci 50:1034–1040

    Article  CAS  Google Scholar 

  29. Nakai S, Li-Chan E, Hayakawa S (1986) Contribution of protein hydrophobicity to its functionality. Food/Nahrung 30:327–336

    Article  CAS  Google Scholar 

  30. Leblanc EL, Leblanc RJ (1992) Determination of hydrophobicity and reactive groups in proteins of cod (Gadus morhua) muscle during frozen storage. Food Chem 43:3–11

    Article  CAS  Google Scholar 

  31. Hayakawa S, Nakai S (1985) Relationships of hydrophobicity and net charge to the solubility of milk and soy protein. J Food Sci 50:486–491

    Article  CAS  Google Scholar 

  32. Niwa E, Kodha S, Kanoh S, Nakayama T (1986) Exposure of hydrophobic amino acid residues from actomyosin on freezing:reconfirmation by fluorometry. Nippon Suisan Gakkaishi 52:1039–1042

    Article  CAS  Google Scholar 

  33. Sano T, Ohno T, Otsuka-Fuchino H, Matsumoto JJ, Tsuchiya T (1994) Carp natural actomyosin: thermal denaturation mechanism. J Food Sci 59:1002–1008

    Article  CAS  Google Scholar 

  34. Damodaran S (1996) Amino acids, peptides and proteins. In: Fennema OR (ed) Food chemistry. Marcel Dekker Inc., New York, pp 321–430

    Google Scholar 

  35. Satoh Y, Nakaya M, Ochiai Y, Watabe S (2006) Characterization of fast skeletal myosin from white croaker in comparison with that from walleye pollack. Fish Sci 72:646–655

    Article  CAS  Google Scholar 

  36. Underland I, Kellerher SD, Hultin HO (2002) Recovery of functional proteins from herring (Clupea harengus) light muscle by an acid or alkaline solubilization process. J Agric Food Chem 50:7371–7379

    Article  Google Scholar 

  37. Offer G, Knight P (1988) The structural basis of water-holding in meat. Part 2: Drip Losses. In: Lawrie R (ed) Developments in meat science. Elsevier Applied Science, London, pp 172–243

  38. Hamm R (1961) Biochemistry of meat hydration. Adv Food Res 10:355–463

    Article  CAS  Google Scholar 

  39. Hamm R (1975) Water-holding capacity of meat. In: Cole DJA, Lawrie RA (eds) Meat, Chap 16. Butterworth, London, p 321

  40. Bertram HC, Kristensen M, Andersen HJ (2004) Functionality of myofibrillar proteins as affected by pH, ionic strength and heat treatment—a low-field NMR study. Meat Sci 68:249–256

    Article  PubMed  CAS  Google Scholar 

  41. Kristinsson HG, Hultin HO (2003) Role of pH and ionic strength on water relationships in washed minced chicken-breast muscle gels. J Food Sci 68:917–922

    Article  CAS  Google Scholar 

  42. Stading M, Hermansson AM (1990) Viscoelastic behavior of beta-lactoglobulin gel structures. Food Hydrocolloid 4:121–135

    Article  CAS  Google Scholar 

  43. Riebroy S, Benjakul S, Visessanguan W, Erikson U, Rustad T (2009) Acid-induced gelation of natural actomyosin from Atlantic cod (Gadus morhua) and burbot (Lota lota). Food Hydrocolloid 23:26–39

    Article  CAS  Google Scholar 

  44. Hermansson AM (1986) Water and fat holding. In: Mitchell JR, Ledward DA (eds) Functional properties of food macromolecules. Elsevier Applied Science Publishing, New York, pp 273–314

    Google Scholar 

  45. Han MY, Fei Y, Xu XL, Zhou GH (2009) Heat-induced gelation of myofibrillar proteins as affected by pH-A low field NMR Study. Sci Agric Sinica 42:2098–2104

    CAS  Google Scholar 

  46. Ptitsyn OB (1995) Molten globule and protein folding. Adv Protein Chem 47:83–229

    Article  PubMed  CAS  Google Scholar 

Download references

Acknowledgments

This work was financially supported by “The National High-tech Research and Development Program of People’s Republic of China (863 Program, No. 2011AA100803)”.

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Authors and Affiliations

  1. School of Food Science and Technology, Dalian Polytechnic University, Dalian, 116034, People’s Republic of China

    Xiu-Ping Dong, Lu-Lu Ma, Ji-Tao Wang, Qiong Wu, Shuang Song & Da-Yong Zhou

  2. National Engineering Research Center of Seafood, Dalian, 116034, People’s Republic of China

    Xiu-Ping Dong, Shuang Song & Da-Yong Zhou

  3. Aquatic Products Processing Laboratory, Liaoning Ocean and Fisheries Science Research Institute, Dalian, 116023, People’s Republic of China

    Jie Zheng

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  1. Xiu-Ping Dong
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Correspondence to Xiu-Ping Dong or Da-Yong Zhou.

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Dong, XP., Ma, LL., Zheng, J. et al. Effect of pH on the physicochemical and heat-induced gel properties of scallop Patinopecten yessoensis actomyosin. Fish Sci 80, 1073–1082 (2014). https://doi.org/10.1007/s12562-014-0778-y

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  • DOI: https://doi.org/10.1007/s12562-014-0778-y

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