Advertisement

Food and Bioprocess Technology

, Volume 12, Issue 2, pp 298–312 | Cite as

Recovery and Extraction of Technofunctional Proteins from Porcine Spleen Using Response Surface Methodology

  • Mònica ToldràEmail author
  • Dolors Parés
  • Elena Saguer
  • Carmen Carretero
Original Paper

Abstract

Porcine spleen is an edible meat by-product from industrial slaughterhouses with a low commercial value that is generally underutilised. In this work, response surface methodology was used to optimise the conditions for protein extraction from porcine spleen. Factors examined were pH (4.3–8.6) and salt concentration (0–4%) of the extraction buffer. The response of several physicochemical characteristics and technofunctional properties of spleen protein fractions as a function of two particular controllable factors of the fractionation process was fitted to second-order polynomial models. The proximate composition (%) of porcine spleen was as follows: moisture (78.9 ± 0.4), protein (17.2 ± 0.7), fat (2.9 ± 0.4), total ash (1.34 ± 0.1) and hydroxyproline (0.20 ± 0.1). Fe content (mg/kg) was 275.5 ± 63. SDS-PAGE patterns of the spleen protein fractions revealed multiple bands with low and high molecular weights from 15 to 220 kDa, corresponding to sarcoplasmic, myofibrillar and connective tissue proteins in both soluble and insoluble fractions with slight differences due to pH and ionic strength extraction conditions. Significant second-order models were obtained for the response variables (protein solubility), foaming and emulsifying properties of soluble fraction, and redness (a*), chroma (C*) and retention properties -cooking loses and water holding capacity- of insoluble residue from porcine spleen. The analysis of the fitted model plots and the ANOVA confirmed that model fits were satisfactory.

Keywords

Animal by-products Porcine spleen Protein extraction Response surface methodology Physicochemical properties Technofunctional properties 

Notes

Acknowledgments

We acknowledge P. Quintana, J. Pernia, X. Morera and A.M. Aymerich for their helpful technical assistance and NORFRISA (Girona, Spain) for the kind donation of the spleen samples.

Funding information

This work was financially supported by the University of Girona (project ref. MPCUdG2016) and the industrial abattoirs: Patel SAU, Olot Meats SL, Friselva SA, NORFRISA, and Frigorífics Costa Brava SA (Girona, Spain), with the financial support of the Government of Catalonia (project ref. 56.21.031.2016 3A).

References

  1. Alao, B., Falowo, A., Chulayo, A., & Muchenje, V. (2017). The potential of animal by-products in food systems: production, prospects and challenges. Sustainability, 9(7), 1089.CrossRefGoogle Scholar
  2. Aluko, R. E., & McIntosh, T. (2001). Polypeptide profile and functional properties of defatted meals and protein isolates of canola seeds. Journal of the Science of Food and Agriculture, 81(4), 391–396.CrossRefGoogle Scholar
  3. Amersham Biosciences. (1998). SDS-PAGE in homogeneous media separation technique file no. 111. Work, 5–10.Google Scholar
  4. AOAC (Association of Official Analytical Chemists). (2000). Official methods of analysis of AOAC international (17th ed.), Arlington, VA, Washington DC. International Association of Official Analytical Chemists. 1141 pp.Google Scholar
  5. Boles, J. A., Rathgeber, B. M., & Shand, P. J. (2000). Recovery of proteins from beef bone and the functionality of these proteins in sausage batters. Meat Science, 55(2), 223–231.CrossRefGoogle Scholar
  6. Carlez, A., Veciana-Nogues, T., & Cheftel, J.-C. (1995). Changes in colour and myoglobin of minced beef meat due to high pressure processing. LWT - Food Science and Technology, 28(5), 528–538.CrossRefGoogle Scholar
  7. Cesta, M. F. (2006). Normal structure, function and histology of the spleen. Toxicologic Pathology, 34(5), 455–465.CrossRefGoogle Scholar
  8. Cortez-Vega, W. R., Fonseca, G. G., & Prentice, C. (2015). Optimization of parameters for obtaining surimi-like material from mechanically separated chicken meat using response surface methodology. Journal of Food Science and Technology, 52(2), 763–772.CrossRefGoogle Scholar
  9. Damodaran, S. (1994). Structure-function relationship of food proteins. In N. S. Hettiarachchy & G. R. Ziegler (Eds.), Protein functionality in food systems (pp. 1–38). New York: Marcel Dekker.Google Scholar
  10. Dàvila, E., Saguer, E., Toldra, M., Carretero, C., & Pares, D. (2007). Surface functional properties of blood plasma protein fractions. European Food Research and Technology, 226(1–2), 207–214.CrossRefGoogle Scholar
  11. Devatkal, S., Mendiratta, S. K., Kondaiah, N., Sharma, M. C., & Anjaneyulu, A. S. R. (2004). Physicochemical, functional and microbiological quality of buffalo liver. Meat Science, 68(1), 79–86.CrossRefGoogle Scholar
  12. Dickinson, E., & Mcclements, D. J. (1996). Advances in food colloids. London: Blackie Academic & Professional.CrossRefGoogle Scholar
  13. EU (European Union). (2005). Commission Regulation (EC) No 2073/2005 of 15 November 2005 of the European parliament and of the Council on Microbiological Criteria for Foodstuffs. Official Journal of the European Union, L338, 1–26. http://eur-lex.europa.eu/eli/reg/2005/2073/oj. Accessed 29 Dec 2017.
  14. FAO. (2009). How to feed the world in 2050. Insights from an Expert Meeting at FAO, 2050(1), 1–35. http://www.fao.org/fileadmin/templates/wsfs/docs/expert_paper/How_to_Feed_the_World_in_2050.pdf.
  15. Fernández-López, J., Sayas-Barberá, E., Pérez-Alvarez, J. A., & Aranda-Catalá, V. (2004). Effect of sodium chloride, sodium tripolyphosphate and pH on color properties of pork meat. Color Research and Application, 29(1), 67–74.CrossRefGoogle Scholar
  16. Fogaça, F. H. S., Trinca, L. A., Bombo, Á. J., & Silvia Sant’Ana, L. (2013). Optimization of the surimi production from mechanically recovered fish meat (MRFM) using response surface methodology. Journal of Food Quality, 36(3), 209–216.CrossRefGoogle Scholar
  17. Gill, C.O. (1988). Microbiology of edible meat by-products. Pearson A.M. and Dutson T.R. (ed.), Edible meat by-products: advances in meat research, volume 5, 47–75. Barking.Google Scholar
  18. Howell, N. K., & Lawrie, R. A. (1983). Functional aspects of blood plasma proteins. I. Separation and characterization. Journal of Food Technology, 18, 747–762.CrossRefGoogle Scholar
  19. Hrynets, Y., Omana, D. A., Xu, Y., & Betti, M. (2011). Comparative study on the effect of acid- and alkaline-aided extractions on mechanically separated turkey meat (MSTM): chemical characteristics of recovered proteins. Process Biochemistry, 46(1), 335–343.CrossRefGoogle Scholar
  20. Jayathilakan, K., Sultana, K., Radhakrishna, K., & Bawa, A. S. (2012). Utilization of byproducts and waste materials from meat, poultry and fish processing industries: a review. Journal of Food Science and Technology, 49(3), 278–293.CrossRefGoogle Scholar
  21. Kang, G., Seong, P., Moon, S., Cho, S., Ham, H., Park, K., & Park, B. (2014). Distribution channel and microbial characteristics of pig by-products in Korea. Korean Journal for Food Science of Animal Resources, 34(6), 792–798.CrossRefGoogle Scholar
  22. Kasankala, L. M., Xue, Y., Weilong, Y., Hong, S. D., & He, Q. (2007). Optimization of gelatine extraction from grass carp (Catenopharyngodon idella) fish skin by response surface methodology. Bioresource Technology, 98(17), 3338–3343.CrossRefGoogle Scholar
  23. Kolar, K. (1990). Colorimetric determination of hydroxyproline as measure of collagen content in meat and meat products: NMKL collaborative study. Journal of the Association of Official Analytical Chemists, 73(1), 54–57.Google Scholar
  24. Leoci, R. (2014). Animal by-products (ABPs): origins, uses, and European regulations. Mantova: Universitas Studiorum S.r.l..Google Scholar
  25. Li, X., Xue, S., Zhao, X., Zhuang, X., Han, M., Xu, X., & Zhou, G. (2018). Gelation properties of goose liver protein recovered by isoelectric solubilisation/precipitation process. International Journal of Food Science and Technology, 53(2), 356–364.CrossRefGoogle Scholar
  26. Luna, E. J., & Hitt, A. L. (1992). Cytoskeleton-plasma membrane interactions. Science, 258(5084), 955–964.CrossRefGoogle Scholar
  27. Lynch, S. A., Alvarez, C., O’Neill, E., Keenan, D. F., & Mullen, A. M. (2017). Optimization of protein recovery from bovine lung by pH shift process using response surface methodology. Journal of the Science of Food and Agriculture, 98, 1951–1960.  https://doi.org/10.1002/jsfa.8678.CrossRefPubMedGoogle Scholar
  28. Lynch, S. A., Mullen, A. M., Neill, E. O., & Álvarez, C. (2018). Opportunities and perspectives for utilisation of co-products in the meat industru. Meat Science, 144, 62–73.CrossRefGoogle Scholar
  29. Mancini, R. A., & Hunt, M. C. (2005). Current research in meat color. Meat Science, 71(1), 100–121.CrossRefGoogle Scholar
  30. Matak, K. E., Tahergorabi, R., & Jaczynski, J. (2015). A review: Protein isolates recovered by isoelectric solubilization/precipitation processing from muscle food by-products as a component of nutraceutical foods. Food Research International, 77, 697–703.CrossRefGoogle Scholar
  31. Morr, C. V., German, B., Kinsella, J. E., Regenstein, J. M., Van Buren, J. P., Kilara, A., Lewis, B. A., & Mangino, M. E. (1985). A collaborative study to develop a standardized food protein solubility procedure. Journal of Food Science, 50(6), 1715–1718.CrossRefGoogle Scholar
  32. Mullen, A. M., Álvarez, C., Zeugolis, D. I., Henchion, M., O’Neill, E., & Drummond, L. (2017). Alternative uses for co-products: harnessing the potential of valuable compounds from meat processing chains. Meat Science, 132, 90–98.CrossRefGoogle Scholar
  33. Neuman, R. E., & Logan, M. A. (1950). The determination of collagen and elastin in tissues. The Journal of Biological Chemistry, 186(2), 549–556.PubMedGoogle Scholar
  34. Nuckles, R. O., Smith, D. M., & Merkel, R. A. (1990). Meat by-product protein composition and functional properties in model systems. Journal of Food Science, 55(3), 640–643.CrossRefGoogle Scholar
  35. Ockerman, H. W., & Hansen, C. L. (1988). Animal by-product processing. Chichester: Ellis Horwood Ltd.Google Scholar
  36. Parés, D. & Ledward, D. A. (2001). Emulsifying and gelling properties of porcine blood plasma as influenced by high-pressure processing. Food Chemistry, 74, 139–145.Google Scholar
  37. Parés, D., Toldrà, M., Saguer, E., & Carretero, C. (2014). Scale-up of the process to obtain functional ingredients based in plasma protein concentrates from porcine blood. Meat Science, 96(1), 304–310.CrossRefGoogle Scholar
  38. Pearce, K. N. & Kinsella, J. E. (1978). Emulsifying properties of proteins - evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry, 26, 716–723.Google Scholar
  39. Pearson, A. M., & Dutson, T. R. (1988). Edible meat by-products, Advances in meat research, volume 5. London: Elsevier Science Publishers Ltd..Google Scholar
  40. Pérez-Chabela, M. L., Soriano-Santos, J., Ponce-Alquicira, E., & Díaz-Tenorio, L. M. (2015). Electroforesis en gel de poliacrilamida-SDS como herramienta en el estudio de las proteínas miofibrilares. Nacameh, 9(2), 77–96.Google Scholar
  41. Rahman, U., Sahar, A., & Khan, M. A. (2014). Recovery and utilization of effluents from meat processing industries. Food Research International, 65, 322–328.CrossRefGoogle Scholar
  42. Rivera, J. A., Sebranek, J. G., Rust, R. E., & Tabatabai, L. B. (2000). Composition and protein fractions of different meat by-products used for petfood compared with mechanically separated chicken (MSC). Meat Science, 55(1), 53–59.CrossRefGoogle Scholar
  43. Selmane, D., Vial, C., & Djelveh, G. (2008). Extraction of proteins from slaughterhouse by-products: Influence of operating conditions on functional properties. Meat Science, 79(4), 640–647.CrossRefGoogle Scholar
  44. Selmane, D., Vial, C., & Djelveh, G. (2010). Production and functional properties of beef lung protein concentrates. Meat Science, 84(3), 315–322.CrossRefGoogle Scholar
  45. Selmane, D., Vial, C., & Djelveh, G. (2011). Emulsification properties of proteins extracted from beef lungs in the presence of xanthan gum using a continuous rotor/stator system. LWT - Food Science and Technology, 44(4), 1179–1188.CrossRefGoogle Scholar
  46. Seong, P. N., Kang, G. H., Park, K. M., Cho, S. H., Kang, S. M., Park, B. Y., & Ba, H. V. (2014a). Characterization of Hanwoo bovine by-products by means of yield, physicochemical and nutritional compositions. Korean Journal for Food Science of Animal Resources, 34(4), 434–447.CrossRefGoogle Scholar
  47. Seong, P. N., Park, K. M., Cho, S. H., Kang, S. M., & Kang, G. H. (2014b). Characterization of edible pork by-products by means of yield and nutritional composition. Korean Journal for Food Science of Animal Resources, 34(3), 297–306.CrossRefGoogle Scholar
  48. Steen, L., Glorieux, S., Goemaere, O., Brijs, K., Paelinck, H., Foubert, I., & Fraeye, I. (2016). Functional properties of pork liver protein fractions. Food and Bioprocess Technology, 9(6), 970–980.CrossRefGoogle Scholar
  49. Sun, X. D., & Holley, R. A. (2011). Factors influencing gel formation by myofibrillar proteins in muscle foods. Comprehensive Reviews in Food Science and Food Safety, 10(1), 33–51.CrossRefGoogle Scholar
  50. Tahergorabi, R., Beamer, S. K., Matak, K. E., & Jaczynski, J. (2011). Effect of isoelectric solubilization/precipitation and titanium dioxide on whitening and texture of proteins recovered from dark chicken-meat processing by-products. LWT - Food Science and Technology, 44(4), 896–903.CrossRefGoogle Scholar
  51. Tahergorabi, R., Sivanandan, L., Beamer, S. K., Matak, K. E., & Jaczynski, J. (2012). A three-prong strategy to develop functional food using protein isolates recovered from chicken processing by-products with isoelectric solubilization/precipitation. Journal of the Science of Food and Agriculture, 92(12), 2534–2542.CrossRefGoogle Scholar
  52. Toldrà, M., Dàvila, E., Saguer, E., Fort, N., Salvador, P., Parés, D., & Carretero, C. (2008). Functional and quality characteristics of the red blood cell fraction from biopreserved porcine blood as influenced by high pressure processing. Meat Science, 80(2), 380–388.CrossRefGoogle Scholar
  53. Toldrà, M., Parés, D., Saguer, E., & Carretero, C. (2011). Hemoglobin hydrolysates from porcine blood obtained through enzymatic hydrolysis assisted by high hydrostatic pressure processing. Innovative Food Science and Emerging Technologies, 12(4), 435–442.CrossRefGoogle Scholar
  54. Toldrá, F., Aristoy, M., Mora, L., & Reig, M. (2012). Innovations in value-addition of edible meat by-products. Meat Science, 92(3), 290–296.CrossRefGoogle Scholar
  55. Toldrá, F., Mora, L., & Reig, M. (2016). New insights into meat by-product utilization. Meat Science, 120, 54–59.CrossRefGoogle Scholar
  56. Xiong, Y. L. (1997). Structure-function relationships of muscle proteins. In S. Damodaran & A. Paraf (Eds.), Food proteins and their applications (pp. 341–392). New York: Marcel Dekker.Google Scholar
  57. Yolmeh, M., & Jafari, S. M. (2017). Applications of response surface methodology in the food industry processes. Food and Bioprocess Technology, 10(3), 413–433.CrossRefGoogle Scholar
  58. Zayas, J. F. (1997). Functionality of proteins in foods. New York: Springer.CrossRefGoogle Scholar
  59. Zhou, C., Wang, H., Chen, Y., & Chen, C. (2012). Effect of L-cysteine and lactose on color stability of porcine red blood cell during freeze-drying and powder storage. Food Science and Biotechnology, 21(3), 669–674.CrossRefGoogle Scholar
  60. Zouari, N., Fakhfakh, N., Amara-Dali, W. B., Sellami, M., Msaddak, L., & Ayadi, M. A. (2011). Turkey liver: Physicochemical characteristics and functional properties of protein fractions. Food and Bioproducts Processing, 89(2), 142–148.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Institute of Food and Agricultural Technology (INTEA), XaRTA, Escola Politècnica Superior (EPS-1)University of GironaGironaSpain

Personalised recommendations