Advertisement

Valorization of Rapeseed Meal: Influence of Ethanol Antinutrients Removal on Protein Extractability, Amino Acid Composition and Fractional Profile

  • Hristo Kalaydzhiev
  • Petya Ivanova
  • Magdalena Stoyanova
  • Atanas Pavlov
  • Turid Rustad
  • Cristina L. M. Silva
  • Vesela I. ChalovaEmail author
Original Paper

Abstract

The production of rapeseed oil leads to generation of large quantities of rapeseed meal as a by-product. To increase the applicability of the rapeseed meal in feed and food industries, the content of antinutrient compounds is often reduced by treatment with ethanol. The aim of the study was to evaluate the influence of ethanol pre-treatment of the rapeseed meal on protein extractability, amino acid composition and fractional profile. The ethanol treatment of the rapeseed meal significantly increased the protein content from 37.4 to 42.3% and reduced the lipid concentration from 1.9 to 1.1%. Approximately 4- and 14-fold reductions of the phenols and glucosinolate contents were achieved respectively. Protein yield, however, was diminished from 26.4 to 23.6%. A stronger decrease of the protein yield, from 47.8 to 26.4%, was caused by processing of the rape seeds to rapeseed meal. The process resulted in the reduction of lysine content, while further ethanol treatment of the rapeseed meal affected more amino acids, both essential (threonine, phenylalanine) and non-essential (alanine, tyrosine, arginine, histidine). Comparative fractional protein profiles of rape seeds, rapeseed meal and ethanol treated rapeseed meal exhibited differences in both composition of the fractions and the relative quantity of the proteins. Data suggested that the treatment of the rapeseed meal with ethanol impacted protein solubility, amino acid composition and protein fractional profile. This knowledge is valuable when ethanol treated rapeseed meal is used either as a protein feed additive or as a source for generation of protein-rich ingredients with specific nutritive value and functionality.

Keywords

Ethanol treatment Amino acid composition Protein extractability Protein fractional profile Rapeseed meal 

Notes

Compliance with Ethical Standards

Conflict of interest

The authors declare that they have no conflict of interest.

Research Involving Animal and Human Participants

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

References

  1. 1.
    Carré, P., Pouzet, A.: Rapeseed market, worldwide and in Europe. OCL 21(1), D102–D114 (2014)CrossRefGoogle Scholar
  2. 2.
    EUBIA Biodiesel market. European Biomass Industry Association, Brussels, Belgium. http://www.eubia.org/cms/wiki-biomass/biofuels-for-transport/biodiesel/. Accessed Sept 2017
  3. 3.
    Ivanova, R.: Rapeseed—The Culture of Present and Future. Videnov & Son, Sofia (2012). ISBN 978-954-8319-59-1306Google Scholar
  4. 4.
    Liu, Y., Zhou, M., Liu, M.: A survey of nutrients and toxic factors in commercial rapeseed meal in China and evaluation of detoxification by water extraction. Anim. Feed Sci. Technol. 45, 257–270 (1994)CrossRefGoogle Scholar
  5. 5.
    Tan, S.H., Mailer, R.J., Blanchard, C.L., Agboola, S.O.: Canola proteins for human consumption: extraction, profile, and functional properties. J. Food Sci. 76, R16–R28 (2011)CrossRefGoogle Scholar
  6. 6.
    Barrett, J.E., Klopfenstein, C.F., Leipold, H.W.: Alkaline heating of canola and rapeseed meals reduces toxicity for chicks. Plant Foods Hum. Nutr. 52, 9–15 (1998)CrossRefGoogle Scholar
  7. 7.
    Gu, X., Dong, W., He, Y.: Detoxification of rapeseed meals by steam explosion. J. Am. Oil Chem. Soc. 88, 1831–1838 (2011)CrossRefGoogle Scholar
  8. 8.
    Vig, A.P., Walia, A.: Beneficial effects of Rhizopus oligosporus fermentation on reduction of glucosinolates, fibre and phytic acid in rapeseed (Brassica napus) meal. Bioresour. Technol. 78, 309–312 (2001)CrossRefGoogle Scholar
  9. 9.
    Shahidi, F., Naczk, M., Hall, D., Synowiecki, J.: Insensitivity of the amino acids of canola and rapeseed to methanol-ammonia extraction and commercial processing. Food Chem. 44, 283–285 (1992)CrossRefGoogle Scholar
  10. 10.
    Ghodsvali, A., Khodaparast, M.H.H., Vosoughi, M., Diosady, L.L.: Preparation of canola protein materials using membrane technology and evaluation of meals functional properties. Food Res. Int. 38, 223–231 (2005)CrossRefGoogle Scholar
  11. 11.
    Purkayastha, M.D., Das, S., Manhar, A.K., Deka, D., Mandal, M., Mahanta, C.L.: Removing antinutrients from rapeseed press-cake and their benevolent role in waste cooking oil-derived biodiesel: conjoining the valorization of two disparate industrial wastes. J. Agric. Food Chem. 61, 10746–10756 (2013)CrossRefGoogle Scholar
  12. 12.
    Adem, H.N., Tressel, R., Pudel, F., Slawski, H., Schulz, C.: Rapeseed use in aquaculture. OCL 21, D105–D114 (2014)CrossRefGoogle Scholar
  13. 13.
    Commission Regulation (EU): № 231/2012. specifications for food additives listed in annexes II and III to regulation (EC) № 1333/2008 of the European Parliament and of the council. Off. J. Eur. Union L83, vol 55Google Scholar
  14. 14.
    Chabanon, G., Chevalot, I., Framboisier, X., Chenu, S., Marc, I.: Hydrolysis of rapeseed protein isolates: kinetics, characterization and functional properties of hydrolysates. Process Biochem. 42, 1419–1428 (2007)CrossRefGoogle Scholar
  15. 15.
    von der Haar, D., Müller, K., Bader-Mittermaier, S., Eisner, P.: Rapeseed proteins—production methods and possible application ranges. OCL 21, D104–D111 (2014)Google Scholar
  16. 16.
    AOAC: Official Methods of Analysis. Association of Official Analytical Chemists, Washington, DC (1990)Google Scholar
  17. 17.
    ICC Standard №104/1: Determination of ash in cereals and cereal products. (1990)Google Scholar
  18. 18.
    ISO 11085: Cereals, cereals-based products and animal feeding stuffs—Determination of crude fat and total fat content by the Randall extraction method, Switzerland (2015)Google Scholar
  19. 19.
    ISO 5489: Agricultural food products—determination of crude fibre content, general method. (1981)Google Scholar
  20. 20.
    Petkova, N., Ivanov, I., Denev, P., Pavlov, A.: Bioactive substance and free radical scavenging activities of flour from Jerusalem artichoke (Helianthus tuberosus L.) tubers—a comparative study. Turk. J. Agric. Nat. Sci., Special Issue 2, 1773–1778 (2014)Google Scholar
  21. 21.
    Ainsworth, E.A., Gillespie, K.M.: Estimation of total phenolic content and other oxidation substrates in plant tissues using Folin–Ciocalteu reagent. Nat. Prot. 2, 875–877 (2007)CrossRefGoogle Scholar
  22. 22.
    Jezek, J., Haggett, B.G.D., Atkinson, A., Rawson, D.M.: Determination of glucosinolates using their alkaline degradation and reaction with ferricyanide. J. Agric. Food Chem. 47, 4669–4674 (1999)CrossRefGoogle Scholar
  23. 23.
    Blackburn, S.: Amino acid determination: methods and techniques. Dekker, New York (1968)Google Scholar
  24. 24.
    Tan, S., Blanchard, C., Mailer, R., Agboola, S.: Extraction and residual antinutritional components in protein fractions of Brassica napus and Sinapis alba oil-free meals. Protein Sci. 21(Suppl. 1), 75–76 (2012)Google Scholar
  25. 25.
    Bradford, M.: A rapid and sensitive for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248–254 (1976)CrossRefGoogle Scholar
  26. 26.
    Laemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685 (1970)CrossRefGoogle Scholar
  27. 27.
    Purkayastha, M., Mahanta, C.L.: Statistically designed optimal process conditions for recuperation of protein from rapeseed meal. J. Food Sci. Technol. 52, 3203–3218 (2015)Google Scholar
  28. 28.
    Ivanova, P., Kalaydzhiev, H., Rustad, T., Silva, C.L.M., Chalova, V.I.: Comparative biochemical profile of protein-rich products obtained from industrial rapeseed meal. Emir. J. Food Agric. 29, 170–178 (2017)CrossRefGoogle Scholar
  29. 29.
    Slawski, H., Adem, H., Tressel, R., Wysujack, K., Koops, U., Kotzamanis, Y., Wuertz, S., Schulz, C.: Total fish meal replacement with rapeseed protein concentrate in diets fed to rainbow trout (Oncorhynchus mykiss Walbaum). Aquacult. Int. 20, 443–453 (2012)CrossRefGoogle Scholar
  30. 30.
    Jensen, S.K., Liu, Y., Eggum, B.O.: The effect of heat treatment on glucosinolates and nutritional value of rapeseed meal in rats. Anim. Feed Sci. Technol. 53, 17–28 (1995)CrossRefGoogle Scholar
  31. 31.
    Mansour, E.H., Dworschák, E., Lugasi, A., Gaál, Ö, Barna, É, Gergely, A.: Effect of processing on the antinutritive factors and nutritive value of rapeseed products. Food Chem. 47, 247–252 (1993)CrossRefGoogle Scholar
  32. 32.
    Fenwick, G.R., Spinks, E., Wilkinson, A.P., Heaney, R.K., Legoy, M.A.: Effect of processing on the antinutrient content of rapeseed. J. Sci. Food Agric. 37, 735–741 (1986)CrossRefGoogle Scholar
  33. 33.
    Dietz, H., King, R., Harris, R.: The aqueous extraction of glucosinolates from rapeseed. Int. J. Food Sci. Technol. 26, 53–63 (1991)CrossRefGoogle Scholar
  34. 34.
    Mosenthin, R., Messerschmidt, U., Sauer, N., Carré, P., Quinsac, A., Schöne, F.: Effect of the desolventizing/toasting process on chemical composition and protein quality of rapeseed meal. J. Anim. Sci. Biotechnol. 7, 36 (2016)CrossRefGoogle Scholar
  35. 35.
    Ivanova, P., Chalova, V., Uzunova, G., Koleva, L., Manolov, I.: Biochemical characterization of industrially produced rapeseed meal as a protein source in food industry. Agric. Agric. Sci. Proc. 10, 55–62: (2016)Google Scholar
  36. 36.
    Bell, J.M., Jeffers, H.F.: Variability in the chemical composition of rapeseed meal. Can. J. Anim. Sci. 56, 269–273 (1976)CrossRefGoogle Scholar
  37. 37.
    Bell, J.M., Keith, M.O.: A survey of variation in the chemical composition of commercial canola meal produced in Western Canadian crushing plants. Can. J. Anim. Sci. 71, 469–480 (1991)CrossRefGoogle Scholar
  38. 38.
    Ayton, J.: Variability of Quality Traits in Canola Seed, Oil and Meal—A Review. NSW Department of Primary Industries, New South Wales (2014)Google Scholar
  39. 39.
    FAO: Nutritional Studies №24 Amino Acid Content of Foods and Biological Data on Proteins. FAO, Rome (1970)Google Scholar
  40. 40.
    Slominski, B., Simbaya, J., Campbell, L., Rakow, G., Guenter, W.: Nutritive value for broilers of meals derived from newly developed varieties of yellow-seeded canola. Anim. Feed Sci. Technol. 78, 249–262 (1999)CrossRefGoogle Scholar
  41. 41.
    Tzeng, Y., Diosady, L.L., Rubin, L.J.: Preparation of rapeseed protein isolates using ultrafiltration, precipitation and diafiltration. Can. Inst. Food.Sci. Technol. J. 21, 419–424 (1988)CrossRefGoogle Scholar
  42. 42.
    Anderson-Hafermann, J.C., Zhang, Y., Parsons, C.M.: Effects of processing on the nutritional quality of canola meal. Poult. Sci. 72, 326–333 (1993)CrossRefGoogle Scholar
  43. 43.
    Wanasundara, J.P.D., McIntosh, T.C., Perera, S.P., Withana-Gamage, T.S., Mitra, P.: Canola/rapeseed protein-functionality and nutrition. OCL 23, D407–D422 (2016)CrossRefGoogle Scholar
  44. 44.
    Agrahar-Murugkar, D., Jha, K.: Effect of drying on nutritional and functional quality and electrophoretic pattern of soyflour from sprouted soybean (Glycine max). J. Food Sci. Technol. 47, 482–487 (2010)CrossRefGoogle Scholar
  45. 45.
    van Koningsveld, G.A., Gruppen, H., de Jongh, H.H., Wijngaards, G., van Boekel, M.A., Walstra, P., Voragen, A.G.: Effects of ethanol on structure and solubility of potato proteins and the effects of its presence during the preparation of a protein isolate. J. Agric. Food Chem. 50, 2947–2956 (2002)Google Scholar
  46. 46.
    Lambrecht, M.A., Rombouts, I., Delcour, J.A.: Denaturation and covalent network formation of wheat gluten, globular proteins and mixtures thereof in aqueous ethanol and water. Food Hydrocoll. 57, 122–131 (2016)CrossRefGoogle Scholar
  47. 47.
    Pace, C.N., Trevino, S., Prabhakaran, E., Scholtz, J.M.: Protein structure, stability and solubility in water and other solvents. Philos. Trans. R. Soc. Lond. B 359, 1225–1235 (2004)Google Scholar
  48. 48.
    Delisle, J., Amiot, J., Goulet, G., Simard, C., Brisson, G.J., Jones, J.D.: Nutritive value of protein fractions extracted from soybean, rapeseed and wheat flours in the rat. Plant Foods Hum. Nutr. 34, 243–251 (1984)Google Scholar
  49. 49.
    Wu, Y.V., Inglett, G.E.: Denaturation of plant proteins related to functionality and food applications. A review. J. Food Sci. 39, 218–225 (1974)Google Scholar
  50. 50.
    Brudzynski, K., Maldonado-Alvarez, L.: Polyphenol-protein complexes and their consequences for the redox activity, structure and function of honey. A current view and new hypothesis—a review. Pol. J. Food Nutr. Sci. 65, 71–80 (2015)Google Scholar
  51. 51.
    Dai, T., Yan, X., Li, Q., Li, T., Liu, C., McClements, D.J., Chen, J.: Characterization of binding interaction between rice glutelin and gallic acid: Multi-spectroscopic analyses and computational docking simulation. Food Res. Int. 102, 274–281 (2017)CrossRefGoogle Scholar
  52. 52.
    Joye, I.J., Davidov-Pardo, G., Ludescher, R.D., McClements, D.J.: Fluorescence quenching study of resveratrol binding to zein and gliadin: Towards a more rational approach to resveratrol encapsulation using water-insoluble proteins. Food Chem. 185, 261–267 (2015)CrossRefGoogle Scholar
  53. 53.
    Aluko, R.E., McIntosh, T.: Polypeptide profile and functional properties of defatted meals and protein isolates of canola seeds. J. Sci. Food Agric. 81, 391–396 (2001)CrossRefGoogle Scholar
  54. 54.
    DuPont, F.M., Chan, R., Lopez, R., Vensel, W.H.: Sequential extraction and quantitative recovery of gliadins, glutenins, and other proteins from small samples of wheat flour. J. Agric. Food Chem. 53, 1575–1584 (2005)CrossRefGoogle Scholar
  55. 55.
    Fu, B., Sapirstein, H.: Procedure for isolating monomeric proteins and polymeric glutenin of wheat flour. Cereal Chem. 73, 143–152 (1996)Google Scholar
  56. 56.
    Huang, A.H.C.: Oil bodies and oleosins in seeds. Ann. Rev. Plant Physiol. Plant Mol. Biol. 43, 177–200 (1992)CrossRefGoogle Scholar

Copyright information

© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular BiologyUniversity of Food TechnologiesPlovdivBulgaria
  2. 2.Department of Analytical Chemistry and PhysicochemistryUniversity of Food TechnologiesPlovdivBulgaria
  3. 3.Laboratory of Applied Biotechnologies, The Stephan Angeloff Institute of MicrobiologyBulgarian Academy of SciencesPlovdivBulgaria
  4. 4.Department of Biotechnology and Food ScienceNorwegian University of Science and TechnologyTrondheimNorway
  5. 5.Escola Superior de BiotecnologiaCBQF -Centro de Biotecnologia e Química Fina – Laboratório AssociadoPortoPortugal

Personalised recommendations