Skip to main content
Log in

Coordination of l-arginine and iron cation improves stability of hemoglobin concentrates

  • Original Paper
  • Published:
European Food Research and Technology Aims and scope Submit manuscript

Abstract

This work evaluated the effects of l-arginine on the stability of porcine hemoglobin concentrates during storage. The addition of l-arginine increased both the oxyhemoglobin content and a* values but decreased both the methemoglobin content and free iron content (p < 0.05) during storage. The addition of iron cation decreased both the oxyhemoglobin content and a* values but increased both the methemoglobin content and free iron content (p < 0.05). CD spectra disclosed that the free iron induced the transformation of the hemoglobin secondary structure from an α-helix to a β-pleated, β-turn, and random-coil arrangement, while l-arginine hindered the behavior of the free iron. Infrared spectra revealed that the l-arginine coordinated with the free Fe2+ or Fe3+ to form the corresponding complex at 25 °C and pH 7.3. These results showed that l-arginine enhanced the stability of hemoglobin concentrates by coordinating with free iron.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5

Similar content being viewed by others

References

  1. Liu YD, Wu HL, Zhang J, Wan DJ, Zhao JH (2012) Study of porcine blood decoloration technique. Adv Mater Res 518–523:3980–3983

    Article  Google Scholar 

  2. Hoyo PD, Rendueles M, Díaz M (2008) Effect of processing on functional properties of animal blood plasma. Meat Sci 78:522–528

    Article  Google Scholar 

  3. Fontes PR, Gomide LAM, Fontes EA, Ramos EM, Ramos ALS (2010) Composition and color stability of carbon monoxide treated dried porcine blood. Meat Sci 85:472–480

    Article  CAS  Google Scholar 

  4. Zhou CL, Ye HQ, Nishiumi T, Qin H, Chen CG (2014) l-Histidine enhances stability of hemoglobin concentrates by coordinating with free iron. Food Res Int 62:637–643

    Article  CAS  Google Scholar 

  5. Zhang HT, Li PJ, Kong BH, Liu Q, Yang HH, Zhao JY, Jiang YN (2013) Effect of glycosylated nitrosohemoglobin on quality of cooked meat batters during chill storage. Adv J Food Sci Technol 5:19–23

    CAS  Google Scholar 

  6. Zhou CL, Wang H, Chen YL, Chen CG (2012) Effect of l-cysteine and lactose on color stability of porcine red blood cell during freeze-drying and powder storage. Food Sci Biotechnol 21:669–674

    Article  CAS  Google Scholar 

  7. Salvador P, Toldrà M, Parés D, Carretero C, Saguer E (2009) Color stabilization of porcine hemoglobin during spray-drying and powder storage by combining chelating and reducing agents. Meat Sci 83:328–333

    Article  CAS  Google Scholar 

  8. Ferrali M, Signorini C, Caciotti B, Sugherini L, Ciccoli L, Giachetti D, Comporti M (1997) Protection against oxidative damage of erythrocyte membrane by the flavonoid quercetin and its relation to iron chelating activity. FEBS Lett 416:123–129

    Article  CAS  Google Scholar 

  9. Waugh WH (2004) Iron chelation by dibasic amino acid prevents glycoprotein insolubilities: a strategy to inhibit age-related macular degeneration? J Appl Res 4:208–214

    CAS  Google Scholar 

  10. Benesch RE, Benesch R, Yung S (1973) Equations for the spectrophotometric analysis of hemoglobin mixtures. Anal Biochem 55:245–248

    Article  CAS  Google Scholar 

  11. Paul C (1971) Spectrophotometric determination of serum iron at the submicrogram level with a new reagent (Ferrozine). Anal Biochem 40:450–458

    Article  Google Scholar 

  12. 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  CAS  Google Scholar 

  13. Gao SL, Chen SP, Yang XW, Shi QZ (2003) Combustion energy and standard molar enthalpy of complexes of the first transition metal chloride and histidine. Chin Sci Bull 48:29–31

    Article  Google Scholar 

  14. Sajadi SAA (2010) Metal ion-binding properties of l-glutamic acid and l-aspartic acid, a comparative investigation. Nat Sci 2:85–90

    CAS  Google Scholar 

  15. Ma F, Chen CG, Zheng L, Zhou CL, Cai KZ, Han Z (2013) Effect of high pressure processing on the gel properties of salt-soluble meat protein containing CaCl2 and κ-carrageenan. Meat Sci 95:22–26

    Article  CAS  Google Scholar 

  16. Livingston DJ, Brown WD (1981) The chemistry of myoglobin and its reactions. Food Technol 35:244–252

    CAS  Google Scholar 

  17. De Nigris F, Lerman LO, Ignarro SW, Sica G, Lerman A, Palinski W, Ignarro LJ, Napoli C (2003) Beneficial effects of antioxidants and l-Arginine on oxidation-sensitive gene expression and endothelial NO synthase activity at sites of disturbed shear stress. PNAS ESI 100:1420–1425

    Article  Google Scholar 

  18. Baker DH (2007) Lysine, arginine and related amino acids: an introduction to the 6th amino acid assessment workshop. J Nutr 137:1599S–1601S

    CAS  Google Scholar 

  19. Rieder RF (1970) Hemoglobin stability: observations on the denaturation of normal and abnormal hemoglobins by oxidant dyes, heat, and alkali. J Clin Invest 49:2369–2376

    Article  CAS  Google Scholar 

  20. Winslow RM (2000) Blood substitutes: refocusing and elusive goal review. Br J Haematol 111:387–396

    Article  CAS  Google Scholar 

  21. Shahidi F, Pegg RB (1991) Novel synthesis of cooked cured-meat pigment. J Food Sci 56:1207–1208

    Google Scholar 

  22. Lester DS, Brumfeld V (1991) Divalent cation-induced changes in conformation of protein kinase C. Biophys Chem 39:215–224

    Article  CAS  Google Scholar 

  23. Tsuruga M, Matsuoka A, Hachimori A, Sugawara Y, Shikama K (1998) The molecular mechanism of autoxidation for human oxyhemoglobin. Tilting of the distal histidine causes nonequivalent oxidation in the beta chain. J Biol Chem 273:8607–8615

    Article  CAS  Google Scholar 

  24. Perutz MF, Kendrew JC, Watson HC (1965) Structure and function of hemoglobin II. Some relations between polypeptide chain configuration and amino acid sequence. J Mol Biol 13:669–678

    Article  CAS  Google Scholar 

  25. Zolghadri S, Saboury AA, Golestani A, Divsalar A, Rezaei-Zarchi S, Moosavi-Movahedi AA (2009) Interaction between silver nanoparticle and bovine hemoglobin at different temperatures. J Nanopart Res 11:1751–1758

    Article  CAS  Google Scholar 

  26. Dunitz J (2001) Pauling’s Left-Handed α-Helix. Angew Chem Int Ed 40:4167–4173

    Article  CAS  Google Scholar 

  27. Jandaruang J, Siritapetawee J, Thumanu K, Songsiriritthigul C, Krittanai C, Daduang S, Dhiravisit A, Thammasirirak S (2012) The effects of temperature and pH on secondary structure and antioxidant activity of Crocodylus siamensis hemoglobin. Protein J 31:43–50

    Article  CAS  Google Scholar 

  28. Platt JR (1953) Classification and assignments of ultraviolet spectra of conjugated organic molecules. J Opt Soc Am 43:252–257

    Article  CAS  Google Scholar 

Download references

Acknowledgments

This research was funded by National Natural Science Foundation of China (21272051) and Anhui Science & Technology Department (1208085C43).

Conflict of interest

There is no conflict of interest.

Compliance with Ethics Requirements

This article does not contain any studies with human or animal subjects.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Cunliu Zhou.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Zhou, C., Ye, H., Wang, H. et al. Coordination of l-arginine and iron cation improves stability of hemoglobin concentrates. Eur Food Res Technol 240, 743–751 (2015). https://doi.org/10.1007/s00217-014-2379-5

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00217-014-2379-5

Keywords

Navigation