Physicochemical Properties of Glycated Chickpea (Cicer Arietinum L.) Protein
Article Sidebar
-
Glycated Chickpea Protein Isolate, Physicochemical Properties
Abstract
Glycated chickpea protein isolate (GCPI) was prepared by the wet-heating method and studied in the present work. The chickpea protein isolate extraction was heated at 80°C for 120 min with the endogenous reducing sugars and oligosaccharides present in the protein extraction (solution). Physicochemical properties of GCPI were also determined. The results showed that the wet-heating method could improve the rate of glycation. The solubility of GCPI was significantly (P < 0.05) higher than that of unglycated chickpea protein isolate (CPI) at the same pH values. The emulsion activity index (EAI) of the GCPI increased remarkably. Furthermore, a significant (P < 0.05) improvement on the emulsifying stability index (ESI) was observed. Little visible flocculation during extended storage (two weeks) was detected.
Full text article
References
[1]-Salunkhe, D. and Deshpande, S. (1991) Introduction. In: Foods of Plant Origin: Production, technology, and human nutrition, ed. D.K. Salunkhe and S.S. Deshpande, An AVI Book, Van Nostrand Reinhold, New York, pp. 1-5.
[2]-Grelda, A.Y.F., Moreno-Valencia, J.G., Falcon-Villa Ma del Refugio and Barron-Hoyos, J. M. (1997)Isolation and partial characterization of starches from dry beans (Phaseolus vulgaris) and chickpeas (Cicer arietinum) grown in Sonora, Mexico. Starch, 49, pp. 341-345.
[3]-Singh, D.G., Abas, A.W., Kaur, D., and Sogi, Singh, D.S. (2008) Characterisation and functional properties of proteins of some Indian chickpea (Cicer arietinum) cultivars. Journal of the Science of Food and Agriculture, 88(5), pp. 778 –786.
[4]-Kaur, M. and Singh, N. (2007)Characterization of protein isolates from different Indian chickpea (Cicer arietinum L.) cultivars. Food Chemistry, 102, pp. 366 –374.
[5]-Santiago Cardoso, R.A., Moreira-Araújo, R.S.R., Pinto de Silva, M.E.M. and Arêas, J.A.G. (2001).The potential of extruded chickpea, corn and bovine lung for malnutrition programs. Innovative Food Science and Emerging Technologies, 2(3), pp. 203 –209.
[6]-Sánchez-Vioque, R., Clemente, A., Vioque, J., Bautista, J. and Millán,F. (1999)Protein isolates from chickpea (Cicer arietinum L.): chemical composition, functional properties and protein characterization. Food Chemistry, 64, pp. 237-243.
[7]-Easa, A., Hill, S. E., Mitchell, J. R., and Taylor, A. J. (1996). Bovine serum albumin gelation as a result of the Maillard reaction. Food Hydrocolloids, 10(2), 199-202.
[8]-Kato, A., Sasaki, Y., Furuta, R., and Kobayashi, K. (1990). Functional protein polysaccharide conjugate prepared by controlled dry-heating of ovalbumin-dextran mixtures. Agricultural and Biological Chemistry, 54(1), 107-112.
[9]-Nakamura, S., Kato, A., and Kobayashi, K. (1992). Enhanced antioxidative effect of ovalbumin due to covalent binding of polysaccharides. Journal of Agricultural and Food Chemistry, 40(11), 2033-2037.
[10]-Cabodevila, O., Hill, S. E., Armstrong, H. J., Sousa, I. and Mitchell, J. R. (1994). Gelation enhancement of soy protein isolate using the Maillard reaction and high temperatures. Journal of Food Science, 59(4), 872-875.
[11]-Saeki, H. (1997). Preparation of neoglycoprotein from carp myofibrillar protein by Maillard reaction with glucose: biochemical properties and emulsifying properties. Journal of Agricultural and Food Chemistry, 45(3), 680-684.
[12]-Darewicz, M., Dziuba, J. and Mioduszewska, H. (1998). Some physico-chemical properties and structural changes of bovine beta-casein upon glycation. Nahrung. 42(3/4): 213-214.
[13]-Kato A., Minaki K., Kobayashi K. (1993): Improvement of emulsifying properties of egg white proteins by the attachment of polysaccharide through Maillard reaction in dry state. Journal of Agricultural and Food Chemistry, 41: 540–543.
[14]-Kato, A., Nakamura, S., Takasaki, H., and Maki, S. (1996). Novel functional properties of glycosylated lysozymes constructed by chemical and genetic modifications. In ACS Symposium. American Chemical Society, Washington. Vol 650, pp 243-256.
[15]-Matsumodi, N., Inoue, Y., Nakashima, H., Kato, A. and Kobayashi, K. (1995). Emulsion stabilization by Maillard-type covalent complex of plasma protein with galactomannan. Journal of Food Science, 60(1), 265-283.
[16]-Shu, Y. W., Sahara, S., Nakamura, S., and Kato, A. (1996). Effects of the length of polysaccharide chains on the functional properties of the Maillard-type lysozyme polysaccharide conjugate. Journal of Agricultural and Food Chemistry, 44(9), 25442548.
[17]-Campbell, L., Euston, S. R., & Ahmed, M. A. (2016). Effect of addition of thermally modified cowpea protein on sensory acceptability and textural properties of wheat bread and sponge cake. Food chemistry, 194, 1230-1237.
[18]-Brands, C. M., Wedzicha, B. L., and van Boekel, M. A. (2002). Quantification of melanoidin concentration in sugar-casein systems. Journal of Agricultural and Food Chemistry, 50(5), 1178-1183.
[19]-Ahmed, M. A. (2013). Investigation of effect of glycation and denaturation on functional properties of cowpea proteins (Doctoral dissertation, Heriot-Watt University).
[20]-Izydorczyk, M. (2005). Understanding the chemistry of food carbohydrates. In: Food carbohydrates: chemistry, physical properties, and applications, ed. by Cui, S.W. Taylor and Francis: New York, pp 44-47.
[21]-Martins, S. I., Jongen, W. M., and Van Boekel, M. A. (2000). A review of Maillard reaction in food and implications to kinetic modelling. Trends in Food Science and Technology, 11(9), 364-373.
[22]-Sikorski, Z. E. (2001). Chemical and Functional properties of Food Proteins. Technomic Publishing Co. Inc., Lancaster-Basel.
[23]-Hayakawa, S., and Nakai, S. (1985). Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. Journal of Food Science, 50(2), 486-491.
[24]-Kobayashi K., Kato A., Matsudomi N. (1990): Developments in novel functional food materials hybridization of soy protein to polysaccharides. Nutrition Science of Soy Protein, Japan, 11: 23–28.
[25]-Comas D.I., Wagner J.R., Tomás M.C. (2006): Creaming stability of oil in water (O/W) emulsions: Influence of pH on soybean protein-lecithin interaction. Food Hydrocolloids, 20: 990–996.
[26]-Dickinson E., Galazka V.B. (1991).Emulsion stabilization by ionic and covalent complexes of β-lactoglobulin with polysaccharides. Food Hydrocolloids, 5: 281–296.
[27]-Diftis N.G., Kiosseoglou V.B. (2003).Improvement of emulsifying properties of soybean protein isolate by conjugation with carboxymethyl cellulose. Food Chemistry: 81: 1–6.
[28]-Felix A., Hill R.A., Diarra B. (1990).in vitro and in vivo digestibility of soya-bean straw treated with various alkalins. Animal Production, 51: 47–60.
Authors
This work is licensed under a Creative Commons Attribution 4.0 International License.
In a brief statement, the rights relate to the publication and distribution of research published in the journal of the University of Sebha where authors who have published their articles in the journal of the university of Sebha should how they can use or distribute their articles. They reserve all their rights to the published works, such as (but not limited to) the following rights:
- Copyright and other property rights related to the article, such as patent rights.
- Research published in the journal of the University of Sebha and used in its future works, including lectures and books, the right to reproduce articles for their own purposes, and the right to self-archive their articles.
- The right to enter a separate article, or for a non-exclusive distribution of their article with an acknowledgment of its initial publication in the journal of Sebha University.
Privacy Statement The names and e-mail addresses entered on the Sabha University Journal site will be used for the aforementioned purposes only and for which they were used.