Waste and Biomass Valorization

, Volume 10, Issue 5, pp 1251–1259 | Cite as

Value-Addition of Defatted Peanut Cake by Proteolysis: Effects of Proteases and Degree of Hydrolysis on Functional Properties and Antioxidant Capacity of Peptides

  • May Kyar Nyo
  • Loc T. NguyenEmail author
Original Paper


In this study, the effects of types of enzymes and degree of hydrolysis on functionalities, DPPH radical scavenging activity, and molecular weight distribution of the peanut protein hydrolysate (PPH) were investigated. Peanut protein was extracted from the oil cake by isoelectric precipitation method. The protein was subjected to controlled hydrolysis using alcalase and pepsin enzymes to yield products with different degrees of hydrolysis (8–17%). The main functional properties of hydrolysates such as solubility, fat absorption capacity (FAC), emulsifying activity index (EAI), emulsifying stability index (ESI) and DPPH radical scavenging activity were determined. Molecular weight distributions were analyzed using SDS-PAGE gel analysis. The results demonstrated that, under studied conditions, the functionalities of PPH were more dependent on types of enzymes than their degrees of hydrolysis. At the same DH, FAC (3.65–3.88 g oil/g PPH) and ESI (71.6–85.2%) of pepsin hydrolysates were higher than FAC (0.58–1.49 g oil/g PPH) and ESI (34.4–50.5%) of alcalase. However, alcalase PPH had better EAI and radical scavenging activity than that of pepsin. Hydrolyzed peanut protein had molecular weights predominantly < 15 kDa. The enzymes used had different specificities toward peanut protein hydrolysis indicated by the distinct molecular weight distribution and functionalities of the corresponding PPH. The findings, to a certain extent, could serve as an important basis for controlling and optimizing peanut protein hydrolysis for specific applications in food industries.

Graphical Abstract


Peanut cake Hydrolysate Enzymatic hydrolysis Functional properties Molecular weight 


  1. 1.
    USDA-FAS. World agricultural production. USDA-FAS, Washington (2015)Google Scholar
  2. 2.
    Jamdar, S., Rajalakshmi, V., Pednekar, M., Juan, F., Yardi, V., Sharma, A.: Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate. Food Chem. 121, 178–184 (2010)CrossRefGoogle Scholar
  3. 3.
    Wu, H., Wang, Q., Ma, T., Ren, J.: Comparative studies on the functional properties of various protein concentrate preparations of peanut protein. Food Res. Int. 42, 343–348 (2009)CrossRefGoogle Scholar
  4. 4.
    Hwang, J.Y., Shyu, Y.S., Wang, Y.T., Hsu, C.K.: Antioxidative properties of protein hydrolysate from defatted peanut kernels treated with esperase. LWT-Food Sci. Technol. 43, 285–290 (2010)CrossRefGoogle Scholar
  5. 5.
    Nwokolo, E., Smartt, J.: Food and feed from oilseeds and legumes. Chapman & Hall Ltd, London (1996)CrossRefGoogle Scholar
  6. 6.
    Mutilangi, W., Panyam, D., Kilara, A.: Functional properties of hydrolysates from proteolysis of heat-denatured whey protein isolate. J. Food Sci. 61, 270–275 (1996)CrossRefGoogle Scholar
  7. 7.
    Zheng, L., Zhao, Y., Xiao, C., Sun-Waterhouse, D., Zhao, M., Su, G.: Mechanism of the discrepancy in the enzymatic hydrolysis efficiency between defatted peanut flour and peanut protein isolate by Flavorzyme. Food Chem. 168, 100–106 (2015)CrossRefGoogle Scholar
  8. 8.
    Korhonen, H.: Milk-derived bioactive peptides: from science to applications. J. Funct. Food 1, 177–187 (2009)CrossRefGoogle Scholar
  9. 9.
    de Castro, R.J.S., Bagagli, M.P., Sato, H.H.: Improving the functional properties of milk proteins: focus on the specificities of proteolytic enzymes. Curr. Opin. Food Sci. 1, 64–69 (2015)CrossRefGoogle Scholar
  10. 10.
    Hou, H., Li, B., Zhao, X., Zhang, Z., Li, P.: Optimization of enzymatic hydrolysis of Alaska pollock frame for preparing protein hydrolysates with low-bitterness. LWT—Food Sci. Technol. 44, 421–428 (2011)Google Scholar
  11. 11.
    Klompong, V., Benjakul, S., Kantachote, D., Shahidi, F.: Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type. Food Chem. 102, 1317–1327 (2007)CrossRefGoogle Scholar
  12. 12.
    Ktari, N., Fakhfakh, N., Balti, R., Ben Khaled, H., Nasri, M., Bougatef, A.: Effect of degree of hydrolysis and protease type on the antioxidant activity of protein hydrolysates from cuttlefish (Sepia officinalis) by-products. J. Aquat. Food Prod. Technol. 22, 436–448 (2013)CrossRefGoogle Scholar
  13. 13.
    Zhao, G., Liu, Y., Zhao, M., Ren, J., Yang, B.: Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate. Food Chem. 127, 1438–1443 (2011)CrossRefGoogle Scholar
  14. 14.
    Shahidi, F., Zhong, Y.: Bioactive peptides. J. AOAC Int. 91, 914–931 (2008)Google Scholar
  15. 15.
    Morais, H.A., Silvestre, M.P.C., Silva, M.R., Silva, V.D.M., Batista, M.A., e Silva, A.C.S., Silveira, J.N.: Enzymatic hydrolysis of whey protein concentrate: effect of enzyme type and enzyme: substrate ratio on peptide profile. J. Food Sci. Technol. 52, 201–210 (2015)CrossRefGoogle Scholar
  16. 16.
    Kristinsson, H.G., Rasco, B.A.: Fish protein hydrolysates: production, biochemical, and functional properties. Crit. Rev. Food Sci. 40, 43–81 (2000)CrossRefGoogle Scholar
  17. 17.
    Gbogouri, G.A., Linder, M., Fanni, J., Parmentier, M.: Influence of hydrolysis degree on the functional properties of salmon byproducts hydrolysates. J. Food Sci. 69, C615-C622 (2004)CrossRefGoogle Scholar
  18. 18.
    Shahidi, F., Han, X.Q., Synowiecki, J.: Production and characteristics of protein hydrolysates from capelin (Mallotus villosus). Food Chem. 53, 285–293 (1995)CrossRefGoogle Scholar
  19. 19.
    Yu, J., Ahmedna, M., Goktepe, I.: Peanut protein concentrate: Production and functional properties as affected by processing. Food Chem. 103, 121–129 (2007)CrossRefGoogle Scholar
  20. 20.
    AOAC: Official methods of analysis of AOAC international, (44th review ed). Association of Official Analytical Chemists, Arlington (1990)Google Scholar
  21. 21.
    Laemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227, 680–685 (1970)CrossRefGoogle Scholar
  22. 22.
    Casella, M.L.A., Whitaker, J.R.: Enzymatically and chemically modified Zein for improvement of functional properties. J Food Biochem. 14, 453–475 (1990)CrossRefGoogle Scholar
  23. 23.
    Pearce, K.N., Kinsella, J.E.: Emulsifying properties of proteins: evaluation of a turbidimetric technique. J. Agric. Food Chem. 26, 716–723 (1978)CrossRefGoogle Scholar
  24. 24.
    Tomotake, H., Shimaoka, I., Kayashita, J., Nakajoh, M., Kato, N.: Physicochemical and functional properties of buckwheat protein product. J. Agric. Food Chem. 50, 2125–2129 (2002)CrossRefGoogle Scholar
  25. 25.
    Shimada, K., Fujikawa, K., Yahara, K., Nakamura, T.: Antioxidative properties of xanthan on the autoxidation of soybean oil in cyclodextrin emulsion. J. Agric. Food Chem. 40, 945–948 (1992)CrossRefGoogle Scholar
  26. 26.
    Rebeca, B.D., Pena-Vera, M.T., Diaz-Castaneda, M.: Production of fish protein hydrolysates with bacterial proteases; Yield and nutritional value. J. Food Sci. 56, 309–314 (1991)CrossRefGoogle Scholar
  27. 27.
    Sugiyama, K., Egawa, M., Onzuka, H., Ôba, K.: Characteristics of sardine muscle hydrolysates prepared by various enzymic treatments. Nippon Suisan Gakkaishi. 57, 475–479 (1991)CrossRefGoogle Scholar
  28. 28.
    Quist, E.E., Phillips, R.D., Saalia, F.K.: The effect of enzyme systems and processing on the hydrolysis of peanut (Arachis hypogaea L.) protein. LWT-Food Sci. Technol. 42, 1717–1721 (2009)CrossRefGoogle Scholar
  29. 29.
    Bianchi-Hall, C.M., Keys, R.D., Stalker, H.T., Murphy, J.P.: Diversity of seed storage protein patterns in wild peanut (Arachis, Fabaceae) species Pl. Syst. Evol. 186, 1–15 (1993)CrossRefGoogle Scholar
  30. 30.
    Parrado, J., Millan, F., Hernandez-Pinzon, I., Bautista, J., Machado, A.: Characterization of enzymic sunflower protein hydrolyzates. J. Agric. Food Chem. 41, 1821–1825 (1993)CrossRefGoogle Scholar
  31. 31.
    Sen, M., Kopper, R., Pons, L., Abraham, E.C., Burks, A.W., Bannon, G.A.: Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes. J. Immunol. 169, 882–887 (2002)CrossRefGoogle Scholar
  32. 32.
    Lawal, O.S.: Functionality of African locust bean (Parkia biglobossa) protein isolate: effects of pH, ionic strength and various protein concentrations. Food Chem. 86, 345–355 (2004)CrossRefGoogle Scholar
  33. 33.
    Tsumura, K., Saito, T., Tsuge, K., Ashida, H., Kugimiya, W., Inouye, K.: Functional properties of soy protein hydrolysates obtained by selective proteolysis. LWT-Food Sci. Technol. 38, 255–261 (2005)CrossRefGoogle Scholar
  34. 34.
    Kotlar, C.E., Ponce, A.G., Roura, S.I.: Improvement of functional and antimicrobial properties of brewery byproduct hydrolysed enzymatically. LWT - Food Sci. Technol. 50, 378–385 (2013)CrossRefGoogle Scholar
  35. 35.
    Panyam, D., Kilara, A.: Enhancing the functionality of food proteins by enzymatic modification. Trends Food Sci. Technol. 7, 120–125 (1996)CrossRefGoogle Scholar
  36. 36.
    del Mar Yust, M., Pedroche, J., del Carmen Millán-Linares, M., Alcaide-Hidalgo, J.M., Millán, F.: Improvement of functional properties of chickpea proteins by hydrolysis with immobilised Alcalase. Food Chem. 122, 1212–1217 (2010)CrossRefGoogle Scholar
  37. 37.
    Taha, F., Ibrahim, M.: Effect of degree of hydrolysis on the functional properties of some oilseed proteins. Grasas Aceites. 53, 273–281 (2002)Google Scholar
  38. 38.
    Gauthier, S., Paquin, P., Pouliot, Y., Turgeon, S.: Surface activity and related functional properties of peptides obtained from whey proteins. J. Dairy Sci. 76, 321–328 (1993)CrossRefGoogle Scholar
  39. 39.
    Tang, C.H., Peng, J., Zhen, D.W., Chen, Z.: Physicochemical and antioxidant properties of buckwheat (Fagopyrum esculentum Moench) protein hydrolysates. Food Chem. 115, 672–678 (2009)CrossRefGoogle Scholar
  40. 40.
    Jun, S.Y., Park, P.J., Jung, W.K., Kim, S.K.: Purification and characterization of an antioxidative peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein. Eur. Food Res. Technol. 219, 20–26 (2004)CrossRefGoogle Scholar
  41. 41.
    Li, B., Chen, F., Wang, X., Ji, B., Wu, Y.: Isolation and identification of antioxidative peptides from porcine collagen hydrolysate by consecutive chromatography and electrospray ionization–mass spectrometry. Food Chem. 102, 1135–1143 (2007)CrossRefGoogle Scholar

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© Springer Science+Business Media B.V., part of Springer Nature 2017

Authors and Affiliations

  1. 1.Food Engineering and Bioprocess TechnologyAsian Institute of TechnologyBangkokThailand

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