Functional properties of protein isolate and acid soluble protein-rich ingredient co-produced from ethanol-treated industrial rapeseed meal

• Autorzy: Kalaydzhiev H. , Ivanova P. , Silva C.L.M. , Chalova V.I.
• Języki publikacji: EN

Abstrakty

EN

Rapeseed meal is produced in large quantities as a by-product of vegetable oil production. To enhance the utility and profitability of the rapeseed meal, it was treated with ethanol and used for concomitant preparation of two protein-rich ingredients, namely protein isolate (PI) and acid soluble protein (ASP). Their functional properties were evaluated in response to two boundary concentrations of NaCl (0.03 and 0.25 mol/L) in a wide pH range (2 to 10). The PI exhibited the lowest protein solubility at isolectric point (pH 4.5) which increased both at lower and higher pH. In contrast, ASP exhibited high protein solubility (>70%) which was negligibly influenced by pH. The addition of 0.03 mol/L NaCl increased its protein solubility to almost 100% at acidic pH. The water holding capacity of PI was positively influenced by the additionf 0.25 mol/L NaCl. The ASP did not exhibit any capacity to hold water but demonstrated higher ability to absorb oil compared to the PI. Both ingredients exhibited different thermal stability in response to salt addition at pH 7 and 8. PI and ASP exhibited completely different pattern of emulsion stability as influenced by pH. While the stability of PI emulsions was close to 100% and only negligibly affected by pH, the ASP emulsion stability significantly varied in response to pH variation. The concomitant production of PI and ASP resulted in products with distinctive techno-functional properties, which makes them suitable for different applications as additives in the formulation of new food products.

• Wydawca: -
• Czasopismo: Polish Journal of Food and Nutrition Sciences
• Rocznik: 2019
• Tom: 69
• Numer: 2
• Opis fizyczny: p.129-136,fig.,ref.

Twórcy

autor

Kalaydzhiev H.

• Department of Biochemistry and Molecular Biology, University of Food Technologies, 26 Maritsa Blvd, Plovdiv 4002, Bulgaria

autor

Ivanova P.

• Department of Biochemistry and Molecular Biology, University of Food Technologies, 26 Maritsa Blvd, Plovdiv 4002, Bulgaria

autor

Silva C.L.M.

• Universidade Catolica Portuguesa, CBQF – Centro de Biotecnologia e Quimica Fina – Laboratorio Associado, Escola Superior de Biotecnologia, Rua Arquiteto Lobao Vital 172, 4200–374 Porto, Portugal

autor

Chalova V.I.

• Department of Biochemistry and Molecular Biology, University of Food Technologies, 26 Maritsa Blvd, Plovdiv 4002, Bulgaria

Bibliografia

• 1. AACC, 1983, Method 46–15: Crude protein – 5-minute Biuret method for wheat and other grains. In: Approved Methods of the American Association of Cereal Chemists, American Association of Cereal Chemists, St. Paul, MN, USA
• 2. Aider, M., Barbana, C. (2011). Canola proteins: composition, extraction, functional properties, bioactivity, applications as a food ingredient and allergenicity – A practical and critical review. Trends in Food Science and Technology, 22(1), 21–39.
• 3. Alashi, A.M., Blanchard, C.L., Mailer, R.J., Agboola, S.O. (2013). Technological and bioactive functionalities of canola meal proteins and hydrolysates. Food Reviews International, 29(3), 231–260.
• 4. Antova, T., Nenkova, G., Georgieva, L. (2008). Comparative investigation of trade marks butter. Scientific Papers, 36, 111–117 [http://blogs.uni-plovdiv.net/argon/files/2008/03/014_NT36_2008.pdf].
• 5. AOAC: Official Methods of Analysis. Association of Official Analytical Chemists, Washington, DC, USA (1990).
• 6. Arntfield, S., Murray, E., Ismond, M. (1986). Effect of salt on the thermal stability of storage proteins from fababean (Vicia faba). Journal of Food Science, 51(2), 371–377.
• 7. Beauchamp, D.L., Khajehpour, M. (2012). Studying salt effects on protein stability using ribonuclease t1 as a model system. Biophysical Chemistry, 161, 29–38.
• 8. Chabanon, G., Chevalot, I., Framboisier, X., Chenu, S., Marc, I. (2007). Hydrolysis of rapeseed protein isolates: Kinetics, characterization and functional properties of hydrolysates. Process Biochemistry, 42(10), 1419–1428.
• 9. Cheung, L., Wanasundara, J., Nickerson, M.T. (2015). Effect of pH and NaCl on the emulsifying properties of a napin protein isolate. Food Biophysics, 10(3), 30–38.
• 10. Das Purkayastha, M., Das, S., Manhar, A.K., Deka, D., Mandal, M., Mahanta, C.L. (2013). Removing antinutrients from rapeseed press-cake and their benevolent role in waste cooking oil-derived biodiesel: Conjoining the valorization of two disparate industrial wastes. Journal of Agricultural and Food Chemistry, 61(45), 10746–10756.
• 11. Das Purkayastha, M., Gogoi, J., Kalita, D., Chattopadhyay, P.,Nakhuru, K.S., Goyary, D., Mahanta, C.L. (2014). Physicochemical and functional properties of rapeseed protein isolate: influence of antinutrient removal with acidified organic solvents from rapeseed meal. Journal of Agricultural and Food Chemistry, 62(31), 7903–7914.
• 12. Dragoev, S.G., Vulkova-Yorgova, K.I., Balev, D.K. (2009). Technology of Functional and Special Meat and Fish Products. Minerva: Sofia, Bulgaria, p. 370, ISBN: 954–24–0053–5 (in Bulgarian).
• 13. FDA, 2018. Approximate pH of foods and food products. [http://ucfoodsafety.ucdavis.edu/files/266402.pdf].
• 14. Fontanari, G.G., Martins, J.M., Kobelnik, M., Pastre, I.A., Arêas, J.A.G., Batistuti, J.P., Fertonani, F.L. (2012). Thermal studies on protein isolates of white lupin seeds (Lupinus albus). Journal of Thermal Analysis and Calorimetry, 108(1), 141–148.
• 15. Ghodsvali, A., Khodaparast, M.H.H., Vosoughi, M., Diosady, L.L. (2005). Preparation of canola protein materials using membrane technology and evaluation of meals functional properties. Food Research International, 2005, 38(2), 223–231.
• 16. González-Pérez, S., Vereijken, J.M. (2007). Sunflower proteins: overview of their physicochemical, structural and functional properties. Journal of the Science of Food and Agriculture, 87(12), 2173–2191.
• 17. Gu, X., Dong, W., He, Y. (2011). Detoxification of rapeseed meals by steam explosion. Journal of the American Oil Chemists Society, 88(11), 1831–1838.
• 18. Ivanova, P., Chalova, V., Koleva, L. (2014). Functional properties of proteins isolated from industrially produced sunflower meal. International Journal of Food Studies, 3, 203–212.
• 19. Ivanova, P., Chalova, V., Koleva, L., Pishtiyski, I. (2013). Amino acid composition and solubility of proteins isolated from sunflower meal produced in Bulgaria. International Food Research Journal, 20, 2995–3000.
• 20. Ivanova, P., Chalova, V., Uzunova, G., Koleva, L., Manolov, I. (2016). Biochemical characterization of industrially produced rapeseed meal as a protein source in food industry. Agricultural Science Procedia, 10, 55–62.
• 21. Ivanova, P., Kalaydzhiev, H., Rustad, T., Silva, C.L.M., Chalova, V.I. (2017). Comparative biochemical profile of protein-rich products obtained from industrial rapeseed meal. Emirates Journal of Food Agriculture, 29(3), 170–178.
• 22. Ivanova, R. (2012). Rapeseed – The Culture of Present and Future. Videnov & Son: Sofia, Bulgaria p. 305, ISBN: 978–954– 8319–59–1 (in Bulgarian).
• 23. Jiang, J., Xiong, Y.L., Chen, J. (2010). pH shifting alters solubility characteristics and thermal stability of soy protein isolate and its globulin fractions in different pH, salt concentration, and temperature conditions. Journal of Agricultural and Food Chemistry, 58(13), 8035–8042.
• 24. Kaushik, J.K., Bhat, R. (1999). A mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions. Protein Science, 8, 222–233.
• 25. Kinsella, J.E., Damodaran, S., German, B. (1985). Physicochemical and functional properties of oilseed proteins with emphasis on soy proteins. In: A.M. Altshul, H.L. Wilcke (eds.). New Protein Foods: Seed Storage Proteins. Academic Press Inc., London, pp.107–179.
• 26. Kreps, F., Vrbiková, L., Schmidt, Š. (2014). Industrial rapeseed and sunflower meal as source of antioxidants. International Journal of Engineering Research and Applications, 4(2), 45–54.
• 27. Li, J., Guo, Z. (2017). Complete utilization of rapeseed meal to produce lipophilic antioxidants, protein, and monosugars in a concordant manner. ACS Sustainable Chemistry & Engineering, 5(7), 6218–6226.
• 28. Lin, C., Zayas, J. (1987). Functionality of defatted corn germ proteins in a model system: fat binding capacity and water retention. Journal of Food Science, 52(5), 1308–1311.
• 29. Lqari, H., Vioque, J., Pedroche, J., Millán, F. (2002). Lupinus angustifolius protein isolates: chemical composition, functional properties and protein characterization. Food Chemistry, 76(3), 349–356.
• 30. Magyar, C., Gromiha, M.M., Sávoly, Z., Simon, I. (2016). The role of stabilization centers in protein thermal stability. Biochemical Biophysical Research Communications, 471(1), 57–62.
• 31. Mao, X., Hua, Y. (2012). Composition, structure and functional properties of protein concentrates and isolates produced from walnut (Juglans regia L.). International Journal of Molecular Sciences, 13(2), 1561–1581.
• 32. Neto, V.Q., Narain, N., Silva, J.B., Bora, P.S. (2001). Functional properties of raw and heat processed cashew nut (Anacardium occidentale, L.) kernel protein isolates. Nahrung-Food, 45(4), 258–262.
• 33. Ogunwolu, S.O., Henshaw, F.O., Mock, H., Santros, A., Awonorin, S.O. (2009). Functional properties of protein concentrates and isolates produced from cashew (Anacardium occidentale L.) nut. Food Chemistry, 115(3), 852–858.
• 34. Okezie, B.O., Bello, A. (1988). Physicochemical and functional properties of winged bean flour and isolate compared with soy isolate. Journal of Food Science, 53(2), 450–454.
• 35. Pegram, L.M., Wendorff, T., Erdmann, R., Shkel, I., Bellissimo, D., Felitsky, D.J., Record, M.T. (2010). Why Hofmeister effects of many salts favor protein folding but not DNA helix formation. Proceedings of the National Academy of Sciences of the United States of Amercia, 107(17), 7716–7721.
• 36. Rodríguez-Ambriz, S., Martínez-Ayala, A., Millán, F., DavilaOrtiz, G. (2005). Composition and functional properties of Lupinus campestris protein isolates. Plant Foods for Human Nutrition, 60(3), 99–107.
• 37. Schnepf, M.I. (1992). Protein-water interactions. In: B.J.F. Hudson (ed.). Biochemistry of Food Proteins. Springer, Boston, MA, USA, pp. 1–33.
• 38. Tang, L., Sun, J., Zhang, H.C., Zhang, C.S., Yu, L.N., Bi, J., Zhu, F., Liu, S.F., Yang, Q.L. (2012). Evaluation of physicochemical and antioxidant properties of peanut protein hydrolysate. PloS One, 7(3), e37863.
• 39. Vioque, J., Sánchez-Vioque, R., Clemente, A., Pedroche, J., Millán, F. (2000). Partially hydrolyzed rapeseed protein isolate with improved functional properties. Journal of the American Oil Chemists Society, 77(4), 447–450.
• 40. Vogt, G., Argos, P. (1997). Protein thermal stability: hydrogen bonds or internal packing? Folding & Design, 2(2), S40-S46.
• 41. Wanasundara, J.P.D., McIntosh, T.C., Perera, S.P., WithanaGamage, T.S., Mitra, P. (2016). Canola/rapeseed protein-functionality and nutrition. OCL – Oilseed and Fats Crops and Lipids, 23(4), D407-D422.
• 42. Xu, L., Diosady, L.L. (1994). Functional properties of Chinese rapeseed protein isolates. Journal of Food Science, 59(5), 1127–1130.
• 43. Yoshie-Stark, Y., Wada, Y., Wäsche, A. (2008). Chemical composition, functional properties, and bioactivities of rapeseed protein isolates. Food Chemistry, 107(1), 32–39.
• 44. Zayas, J.F. (1997). Solubility of proteins. In: Functionality of Proteins in Food. Springer-Verlag, Heidelberg, Germany, pp.6–75 ISBN: 978–3-642–63856–5.
• 45. Zentková, I., Cvengrošová, E. (2013). The utilization of rapeseed for biofuels production in the EU. Visegrad Journal of Bioeconomy and Sustainable Development, 2, 11–14.

Identyfikatory

DOI

10.31883/pjfns-2019-0007