[en] The main purpose of this work was to investigate some physiochemical and antioxidant properties of purified proteins of 18 kDa from black cumin seeds. The structural properties of purified proteins were characterized using Fourier Transform-Infrared spectroscopy (FT-IR) and Circular dichroism (CD) spectroscopy analysis. The Tunisian purified protein exhibited a α-helix structure and the Turkish purified protein adopted a β-sheet conformation. The thermal properties were also evaluated by differential scanning calorimetry (DSC). The Tunisian purified protein presented two endothermic peaks, the first one was at 76.71 °C and the second one was at 131.32 °C. However, only one endothermic peak was found for the Turkish purified protein at 157.63 °C. Both Tunisian and Turkish purified proteins were very stable towards heat-induced denaturation. In addition, the effect of pH, salt (NaCl and Na(2)SO(4)) and temperature on functional properties was investigated. The Tunisian black cumin seeds pure protein exhibited better antioxidant activity than that of the Turkish one at all tested concentrations (0.2 to 1 mg/mL) and temperatures (50 °C, 75 °C and 100 °C), as well as after gastrointestinal digestion simulation.
Disciplines :
Food science
Author, co-author :
Trigui, Ines; Laboratoire de Valorisation, Analyses et Sécurité des Aliments, Université de Sfax, École Nationale d'Ingénieurs de Sfax, Route de Soukra, 3038 Sfax, Tunisia. Electronic address: inestrigui89@gmail.com.
Zarai, Zied; Laboratoire de Biochimie et de Génie Enzymatique des Lipases, Université de Sfax, École Nationale d'Ingénieurs de Sfax, Route de Soukra, 3038 Sfax, Tunisia.
Chevance, Soizic; UMR 6226 CNRS Equipe Ingénierie Chimique et Molécules pour le Vivant, Université de Rennes 1, Institut des Sciences Chimiques de Rennes, Campus Scientifique de Beaulieu, 263 av du Général Leclerc, 35042 Rennes Cedex, France.
Cheikh-Rouhou, Salma; Laboratoire de Valorisation, Analyses et Sécurité des Aliments, Université de Sfax, École Nationale d'Ingénieurs de Sfax, Route de Soukra, 3038 Sfax, Tunisia.
Attia, Hamadi; Laboratoire de Valorisation, Analyses et Sécurité des Aliments, Université de Sfax, École Nationale d'Ingénieurs de Sfax, Route de Soukra, 3038 Sfax, Tunisia.
Ayadi, Mohamed ; Laboratoire de Valorisation, Analyses et Sécurité des Aliments, Université de Sfax, École Nationale d'Ingénieurs de Sfax, Route de Soukra, 3038 Sfax, Tunisia.
Language :
English
Title :
Physicochemical properties, antioxidant activity and in vitro gastrointestinal digestion of purified proteins from black cumin seeds.
Publication date :
01 April 2019
Journal title :
International Journal of Biological Macromolecules
Randhawa, M.A., Black seed, Nigella sativa, deserves more attention. J. Ayub Med. Coll. Abbottabad 20 (2008), 1–2.
Trigui, I., Yaich, H., Sila, A., Cheikh-Rouhou, S., Bougatef, A., Blecker, C., Attia, H., Ayadi, M.A., Physicochemical properties of water-soluble polysaccharides from black cumin seeds. Int. J. Biol. Macromol. 117 (2018), 937–946.
Salem, M.L., Immunomodulatory and therapeutic properties of the Nigella sativa L. seed. Int. Immunopharmacol. 5 (2005), 1749–1770.
Maulik, S.K., Kumar, S., Oxidative stress and cardiac hypertrophy: a review. Toxicol. Mech. Methods 22 (2012), 359–366.
Wardhani, D.H., Fuciños, P., Vázquez, J.A., Pandiella, S.S., Inhibition kinetics of lipid oxidation of model foods by using antioxidant extract of fermented soybeans. Food Chem. 139 (2013), 837–844.
Power, O., Jakeman, P., FitzGerald, R.J., Antioxidative peptides: enzymatic production, in vitro and in vivo antioxidant activity and potential applications of milk-derived antioxidative peptides. Amino Acids 44 (2013), 797–820.
Ito, N., Fukushima, S., Tsuda, H., Carcinogenicity and modification of the carcinogenic response by BHA, BHT, and other antioxidants. CRC Crit. Rev. Toxicol. 15 (1985), 109–150.
El-Shourbagy, G.A., El-Zahar, K.M., Oxidative stability of ghee as affected by natural antioxidants extracted from food processing wastes. Ann. Agric. Sci. 59 (2014), 213–220.
Senanayake, S.P.J.N., Green tea extract: chemistry, antioxidant properties and food applications—a review. J. Funct. Foods 5 (2013), 1529–1541.
Amir, M., Dar, M.A., Haque, M.A., Islam, A., Ahmad, F., Hassan, M.I., Purification and characterization of Ras related protein, Rab5a from Tinospora cordifolia. Int. J. Biol. Macromol. 82 (2016), 471–479.
Bojórquez-Velázquez, E., Lino-López, G.J., Huerta-Ocampo, J.A., Barrera-Pacheco, A., de la Rosa, A.P.B., Moreno, A., Mancilla-Margalli, N.A., Osuna-Castro, J.A., Purification and biochemical characterization of 11S globulin from chan (Hyptis suaveolens L. Poit) seeds. Food Chem. 192 (2016), 203–211.
Cortés-Giraldo, I., Megías, C., Alaiz, M., Girón-Calle, J., Vioque, J., Purification of free arginine from chickpea (Cicer arietinum) seeds. Food Chem. 192 (2016), 114–118.
Campos, D.C.O., Costa, A.S., Lima, A.D.R., Silva, F.D.A., Lobo, M.D.P., Monteiro-Moreira, A.C.O., Moreira, R.A., Leal, L.K.A.M., Miron, D., Vasconcelos, I.M., First isolation and antinociceptive activity of a lipid transfer protein from noni (Morinda citrifolia) seeds. Int. J. Biol. Macromol. 86 (2016), 71–79.
Wierenga, P.A., Gruppen, H., New views on foams from protein solutions. Curr. Opin. Colloid Interface Sci. 15 (2010), 365–373.
AOAC, Official Methods of Analysis of the Association of Official Analytical Chemists. 1997, AOAC, Virginia, USA.
LaemmLi, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970), 680–685.
Wani, I.A., Sogi, D.S., Gill, B.S., Original article physical and cooking characteristics of black gram (Phaseolus mungoo L.) cultivars grown in India. Int. J. Food Sci. Technol. 48 (2013), 2557–2563.
Pearce, K.N., Kinsella, J.E., Emulsifying properties of proteins: evaluation of a turbidimetric technique. J. Agric. Food Chem. 26 (1978), 716–723.
Coffmann'll, C.W., Garclai, V.V., Functional properties and amino acid content of a protein isolate from mung bean flour. Int. J. Food Sci. Technol. 12 (1977), 473–484.
Mcconnell, A.A., Eastwood, M.A., Mitchell, W.D., Physical characteristics of vegetable foodstuffs that could influence bowel function. J. Sci. Food Agric. 25 (1974), 1457–1464.
Lin, M.J.-Y., Humbert, E.S., Sosulski, F.W., Certain functional properties of sunflower meal products. J. Food Sci. 39 (1974), 368–370.
Bersuder, P., Hole, M., Smith, G., Antioxidants from a heated histidine–glucose model system. I: investigation of the antioxidant role of histidine and isolation of antioxidants by high-performance liquid chromatography. J. Am. Oil Chem. Soc. 75 (1998), 181–187.
Yıldırım, A., Mavi, A., Bo, B., Determination of antioxidant and antimicrobial activities of Rumex crispus L. extracts. J. Agric. Food Chem. 49 (2001), 4083–4089.
Decker, E.A., Welch, B., Role of ferritin as a lipid oxidation catalyst in muscle food. J. Agric. Food Chem. 38 (1990), 674–677.
Enari, H., Takahashi, Y., Kawarasaki, M., Tada, M., Tatsuta, K., Identification of angiotensin I-converting enzyme inhibitory peptides derived from salmon muscle and their antihypertensive effect. Fish. Sci. 74 (2008), 911–920.
Cheikh-Rouhou, S., Besbes, S., Hentati, B., Blecker, C., Deroanne, C., Attia, H., Nigella sativa L.: chemical composition and physicochemical characteristics of lipid fraction. Food Chem. 101 (2007), 673–681.
Gorjanović S., Spillner, E., Beljanski, M.V., Gorjanović R., Pavlović M., Gojgić-Cvijanović G., Malting barley grain non-specific lipid-transfer protein (ns-LTP): importance for grain protection. J. Inst. Brew. 111 (2005), 99–104.
Schuler, B., Kremer, W., Kalbitzer, H.R., Jaenicke, R., Role of entropy in protein thermostability: folding kinetics of a hyperthermophilic cold shock protein at high temperatures using 19F NMR. Biochemistry 41 (2002), 11670–11680.
Haque, M.A., Zaidi, S., Ubaid-ullah, S., Prakash, A., Hassan, M.I., Islam, A., Batra, J.K., Ahmad, F., In vitro and in silico studies of urea-induced denaturation of yeast iso-1-cytochrome c and its deletants at pH 6.0 and 25 °C. J. Biomol. Struct. Dyn. 33 (2015), 1493–1502.
Degli Esposti, M., Ballester, F., Solaini, G., Lenaz, G., The circular-dichroic properties of the ‘Rieske’ iron-sulphur protein in the mitochondrial ubiquinol: cytochrome c reductase. Biochem. J. 241 (1987), 285–290.
Li, R., Nagai, Y., Nagai, M., Changes of tyrosine and tryptophan residues in human hemoglobin by oxygen binding: near-and far-UV circular dichroism of isolated chains and recombined hemoglobin. J. Inorg. Biochem. 82 (2000), 93–101.
Greenfield, N.J., Using circular dichroism spectra to estimate protein secondary structure. Nat. Protoc., 1, 2006, 2876.
Galdino, A.S., Silva, R.N., Lottermann, M.T., Alvares, A.C.M., de Moraes, L.M.P., Torres, F.A.G., de Freitas, S.M., Ulhoa, C.J., Biochemical and structural characterization of Amy1: an alpha-amylase from Cryptococcus flavus expressed in Saccharomyces cerevisiae. Enzyme Res., 2011, 2011.
Haug, I.J., Skar, H.M., Vegarud, G.E., Langsrud, T., Draget, K.I., Electrostatic effects on β-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry. Food Hydrocoll. 23 (2009), 2287–2293.
Siu, N.-C., Ma, C.-Y., Mine, Y., Physicochemical and structural properties of oat globulin polymers formed by a microbial transglutaminase. J. Agric. Food Chem. 50 (2002), 2660–2665.
Jin, T., Wang, Y., Chen, Y.-W., Albillos, S.M., Kothary, M.H., Fu, T.-J., Tankersley, B., McHugh, T.H., Zhang, Y.-Z., Isolation and characterization of Korean pine (Pinus koraiensis) convicilin. Plant Physiol. Biochem. 80 (2014), 97–104.
Marques, C., Viegas, F., Rito, J., Jones, J., Viegas, I., Determination of muscle protein synthesis rates in fish using 2H2O and 2H NMR analysis of alanine. Anal. Biochem. 509 (2016), 111–114.
Vidal, N.P., Picone, G., Goicoechea, E., Laghi, L., Manzanos, M.J., Danesi, F., Bordoni, A., Capozzi, F., Guillén, M.D., Metabolite release and protein hydrolysis during the in vitro digestion of cooked sea bass fillets. A study by 1H NMR. Food Res. Int. 88 (2016), 293–301.
Santoni, I., Pizzo, B., Evaluation of alternative vegetable proteins as wood adhesives. Ind. Crop. Prod. 45 (2013), 148–154.
Jackson, M., Haris, P.I., Chapman, D., Fourier transform infrared spectroscopic studies of calcium-binding proteins. Biochemistry 30 (1991), 9681–9686.
Song, C.-L., Zhao, X.-H., Structure and property modification of an oligochitosan-glycosylated and crosslinked soybean protein generated by microbial transglutaminase. Food Chem. 163 (2014), 114–119.
Kong, J., Yu, S., Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochim. Biophys. Sin. 39 (2007), 549–559.
Sikorski, Zdzis.E., Functional properties of proteins in food systems. Chem. Funct. Prop. Food Proteins, 2001, 113–136.
Guan, X., Yao, H., Chen, Z., Shan, L., Zhang, M., Some functional properties of oat bran protein concentrate modified by trypsin. Food Chem. 101 (2007), 163–170.
Karaca, A.C., Low, N., Nickerson, M., Emulsifying properties of chickpea, faba bean, lentil and pea proteins produced by isoelectric precipitation and salt extraction. Food Res. Int. 44 (2011), 2742–2750.
Wang, J.C., Kinsella, J.E., Functional properties of novel proteins: alfalfa leaf protein. J. Food Sci. 41 (1976), 286–292.
Puppo, M.C., Sorgentini, D.A., Añón, M.C., Rheological properties of emulsions containing modified soy protein isolates. J. Am. Oil Chem. Soc. 80 (2003), 605–611.
Makri, E., Papalamprou, E., Doxastakis, G., Study of functional properties of seed storage proteins from indigenous European legume crops (lupin, pea, broad bean) in admixture with polysaccharides. Food Hydrocoll. 19 (2005), 583–594.
Hang, Y.D., Steinkraus, K.H., Hackler, L.R., Comparative studies on the nitrogen solubility of mung beans, pea beans and red kidney beans. J. Food Sci. 35 (1970), 318–320.
Erdem, Y.K., Modification of casein micelle structure caused by ultrafiltration and heat treatment: a spectrofluorimetric and kinetic approach. J. Food Eng. 74 (2006), 536–541.
López, D.N., Ingrassia, R., Busti, P., Bonino, J., Delgado, J.F., Wagner, J., Boeris, V., Spelzini, D., Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds. LWT Food Sci. Technol. 90 (2018), 396–402.
Hu, H., Fan, T., Zhao, X., Zhang, X., Sun, Y., Liu, H., Influence of pH and salt concentration on functional properties of walnut protein from different extraction methods. J. Food Sci. Technol. 54 (2017), 2833–2841.
Kaushik, P., Dowling, K., Adhikari, R., Barrow, C.J., Adhikari, B., Effect of extraction temperature on composition, structure and functional properties of flaxseed gum. Food Chem. 215 (2017), 333–340.
Číž M., Čížová H., Denev, P., Kratchanova, M., Slavov, A., Lojek, A., Different methods for control and comparison of the antioxidant properties of vegetables. Food Control 21 (2010), 518–523.
Kou, X., Gao, J., Xue, Z., Zhang, Z., Wang, H., Wang, X., Purification and identification of antioxidant peptides from chickpea (Cicer arietinum L.) albumin hydrolysates. LWT Food Sci. Technol. 50 (2013), 591–598.
Guerard, F., Sumaya-Martinez, M.T., Laroque, D., Chabeaud, A., Dufossé L., Optimization of free radical scavenging activity by response surface methodology in the hydrolysis of shrimp processing discards. Process Biochem. 42 (2007), 1486–1491.
De Wit, J.N., Thermal behaviour of bovine β-lactoglobulin at temperatures up to 150 °C. A review. Trends Food Sci. Technol. 20 (2009), 27–34.
de Castro, R.J.S., Sato, H.H., A response surface approach on optimization of hydrolysis parameters for the production of egg white protein hydrolysates with antioxidant activities. Biocatal. Agric. Biotechnol. 4 (2015), 55–62.
