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Original Research | Open Access

Antioxidant properties of camelina (Camelina sativa (L.) Crantz) protein hydrolysates

Na Thi Ty Ngo()Fereidoon Shahidi
Department of Biochemistry, Memorial University of Newfoundland, St. John's, NL, Canada A1C 5S7
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Abstract

Camelina seed meal was used to produce protein hydrolysates using Alcalase and Flavourzyme. The hydrolysates were then fractionated by employing ultrafiltration membranes (3, 10 kDa). The antioxidant activities of camelina protein hydrolysates and peptide fractions were investigated. The essential amino acid content of camelina protein isolates and hydrolysates was comparable and adequate. All camelina hydrolysates exhibited the highest radical scavenging activity in both DPPH and ABTS assay compared to camelina protein isolates. When comparing the overall DPPH and ABTS radical scavenging activity of peptide fractions, smaller-size peptides (< 3 kDa) displayed considerably higher values and hence more potency than larger-sized peptides (> 3 kDa). Peptide fractions with 3–10 kDa had better metal chelation and reducing power than those < 3 kDa and > 10 kDa. These findings suggest that camelina protein hydrolysates could be employed as bioactive ingredients in the formulation of functional foods and against oxidative stress.

References

 

Alashi, A.M., Blanchard, C.L., Mailer, R.J., Agboola, S.O., Mawson, A.J., He, R., and Aluko, R.E. (2014). Antioxidant properties of Australian canola meal protein hydrolysates. Food Chem. 146: 500–506.

 

Aluko, R.E., and Monu, E. (2003). Functional and Bioactive Properties of Qui-noa Seed Protein Hydrolysates. J. Food Sci. 68: 1254–1258.

 

Ambigaipalan, P., Al-Khalifa, A.S., and Shahidi, F. (2015). Antioxidant and an-giotensin I converting enzyme (ACE) inhibitory activities of date seed protein hydrolysates prepared using Alcalase, Flavourzyme and Ther-molysin. J. Funct. Foods 18: 1125–1137.

 

Ambigaipalan, P., and Shahidi, F. (2017). Bioactive peptides from shrimp shell processing discards: Antioxidant and biological activities. J. Funct. Foods 34: 7–17.

 

Boyle, C., Hansen, L., Hinnenkamp, C., and Ismail, B.P. (2018). Emerging Camelina Protein: Extraction, Modification, and Structural/Functional Characterization. J. Am. Oil Chem. Soc. 95(8): 1049–1062.

 

Carlos, M.G.A., Walter, M., and Jonh, J.M.A. (2017). Antioxidant potential use of bioactive peptides derived from mung bean hydrolysates (Vigna Radiata). African J. Food Sci. 11(3): 67–73.

 

Chandrasekara, A., and Shahidi, F. (2011). Inhibitory activities of soluble and bound millet seed phenolics on free radicals and reactive oxygen spe-cies. J. Agr. Food Chem. 59(1): 428–436.

 

Cumby, N., Zhong, Y., Naczk, M., and Shahidi, F. (2008). Antioxidant activity and water-holding capacity of canola protein hydrolysates. Food Chem. 109(1): 144–148.

 

Girgih, A.T., Udenigwe, C.C., and Aluko, R.E. (2011). In Vitro Antioxidant Properties of Hemp Seed (Cannabis sativa L. ) Protein Hydrolysate Frac-tions. J. Am. Oil Chem. Soc. 88(3): 381–389.

 

He, R., Girgih, A.T., Malomo, S.A., Ju, X., and Aluko, R.E. (2013). Antioxidant activities of enzymatic rapeseed protein hydrolysates and the mem-brane ultrafiltration fractions. J. Funct. Foods 5(1): 219–227.

 

Hixson, S.M., Parrish, C.C., Wells, J.S., Winkowski, E.M., Anderson, D.M., and Bullerwell, C.N. (2016). Inclusion of camelina meal as a protein source in diets for farmed salmonids. Aquac. Nutr. 22(3): 615–630.

 

Hu, R., Chen, G., and Li, Y. (2020). Production and Characterization of An-tioxidative Hydrolysates and Peptides from Corn Gluten Meal Using Papain, Ficin, and Bromelain. Molecules 25(18): 4091.

 

Intarasirisawat, R., Benjakul, S., Visessanguan, W., and Wu, J. (2012). Antioxi-dative and functional properties of protein hydrolysate from defatted skipjack (Katsuwonous pelamis) roe. Food Chem. 135(4): 3039–3048.

 

John, J.A., and Shahidi, F. (2010). Phenolic compounds and antioxidant activ-ity of Brazil nut (Bertholletia excelsa). J. Funct. Foods 2(3): 196–209.

 

Kristinsson, H.G., and Rasco, B.A. (2000). Fish protein hydrolysates: produc-tion, biochemical, and functional properties. Crit. Rev. Food Sci. Nutr. 40(1): 43–81.

 

Li, N., Qi, G., Sun, X.S., Wang, D., Bean, S., and Blackwell, D. (2014). Isola-tion and Characterization of Protein Fractions Isolated from Camelina Meal. Am. Soc. Agr. Biol. Eng. 57: 169–178.

 

Li, N., Qi, G., Sun, X.S., Xu, F., and Wang, D. (2015). Adhesion properties of camelina protein fractions isolated with different methods. Ind. Crops Prod. 69: 263–272.

 

Mohan, A., and Udenigwe, C.C. (2015). Towards the design of hypolipidae-mic peptides: Deoxycholate binding affinity of hydrophobic peptide aggregates of casein plastein. J. Funct. Foods 18: 129–136.

 

Mundi, S., and Aluko, R.E. (2014). Inhibitory Properties of Kidney Bean Pro-tein Hydrolysate and its Membrane Fractions Against Renin, Angioten-sin Converting Enzyme, and Free Radicals. Austin J. Nutr. Food Sci. 2(1): 1008.

 

Ngo, N.T.T., and Shahidi, F. (2021). Functional properties of protein isolates from camelina (Camelina sativa (L. ) Crantz) and flixweed (sophia, Descurainis sophia L. ) seed meals. Food Prod. Proc. Nutr. 3(1): 31.

 

Russo, R., and Reggiani, R. (2015). Seed Protein in Camelina sativa (L. ) Crantz var. Calena. Int. J. Plant and Soil Sci. 8(2): 1–6.

 

Senadheera, T.R.L., Dave, D., and Shahidi, F. (2021). Antioxidant potential and physicochemical properties of protein hydrolysates from body parts of North Atlantic sea cucumber (Cucumaria frondosa). Food Prod. Proc. Nutr. 3(1): 3.

 

Shahidi, F., and Yeo, J. (2020). Should the in vitro colorimetric assays in anti-oxidant and lipid oxidation evaluation be abandoned? A critical review focusing on bioactive molecule screening assays in in vitro and in vivo models. J. Food Bioact. 9: 23–35.

 

Shahidi, F., and Zhong, Y. (2015). Measurement of antioxidant activity. J. Funct. Foods 18: 757–781.

 

Tavarini, S., De Leo, M., Matteo, R., Lazzeri, L., Braca, A., and Angelini, L.G. (2021). Flaxseed and Camelina Meals as Potential Sources of Health-Beneficial Compounds. Plants (Basel) 10(1): 156.

 

Udenigwe, C.C., and Aluko, R.E. (2011). Chemometric analysis of the amino acid requirements of antioxidant food protein hydrolysates. Int. J. Mol. Sci. 12(5): 3148–3161.

 

Udenigwe, C.C., and Aluko, R.E. (2012). Food protein-derived bioactive pep-tides: production, processing, and potential health benefits. J. Food Sci. 77(1): 11–24.

 

Udenigwe, C.C., Udechukwu, M.C., Yiridoe, C., Gibson, A., and Gong, M. (2016). Antioxidant mechanism of potato protein hydrolysates against in vitro oxidation of reduced glutathione. J. Funct. Foods 20: 195–203.

 

Zou, T.B., He, T.P., Li, H.B., Tang, H.W., and Xia, E.Q. (2016). The Structure-Ac-tivity Relationship of the Antioxidant Peptides from Natural Proteins. Molecules 21(1): 72.

Journal of Food Bioactives
Pages 75-82
Cite this article:
Ngo NTT, Shahidi F. Antioxidant properties of camelina (Camelina sativa (L.) Crantz) protein hydrolysates. Journal of Food Bioactives, 2021, 16: 75-82. https://doi.org/10.31665/JFB.2021.16295
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