Recovery and Extraction of Technofunctional Proteins from Porcine Spleen Using Response Surface Methodology
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.
KeywordsAnimal by-products Porcine spleen Protein extraction Response surface methodology Physicochemical properties Technofunctional properties
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.
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).
- Amersham Biosciences. (1998). SDS-PAGE in homogeneous media separation technique file no. 111. Work, 5–10.Google Scholar
- 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
- 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
- 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.
- 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.
- 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
- 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
- Leoci, R. (2014). Animal by-products (ABPs): origins, uses, and European regulations. Mantova: Universitas Studiorum S.r.l..Google Scholar
- 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
- Ockerman, H. W., & Hansen, C. L. (1988). Animal by-product processing. Chichester: Ellis Horwood Ltd.Google Scholar
- 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
- 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
- Pearson, A. M., & Dutson, T. R. (1988). Edible meat by-products, Advances in meat research, volume 5. London: Elsevier Science Publishers Ltd..Google Scholar
- 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
- 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
- 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
- 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
- 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