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Original Articles

Structural and Functional Properties of Ovalbumin Glycated by Dry-Heating in the Presence of Maltodextrin

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Pages 1326-1333 | Received 09 Aug 2011, Accepted 31 Aug 2011, Published online: 03 Mar 2015

REFERENCES

  • Choi, S.M.; Ma, C.Y. Structural characterization of globulin from common buckwheat (Fagopyrum esculentum Moench) using circular dichroism and Raman spectroscopy. Food Chemistry 2007, 102, 150–160.
  • Alamprese, C.; Iametti, S.; Rossi, M.; Bergonzi, D. Role of pasteurisation heat treatments on rheological and protein structural characteristics of fresh egg pasta. European Food Research and Technology 2005, 221, 759–767.
  • Mulsow, B.B.; Jacob, M.; Henle, T. Studies on the impact of glycation on the denaturation of whey proteins. European Food Research and Technology 2009, 228, 643–649.
  • Kato, A.; Ibrahim, H.R.; Takagi, T.; Kobayashi, K. Excellent gelation of egg-white preheated in the dry state is due to the decreasing degree of aggregation. Journal of Agricultural and Food Chemistry 1990, 38, 1868–1872.
  • Hellwig, M.; Henle, T. Formyline, a new glycation compound from the reaction of lysine and 3-deoxypentosone. European Food Research and Technology 2010, 230, 903–914.
  • Miguel, M.; Manso, M.A.; Lopez, F.R.; Ramos, M. Comparative study of egg white proteins from different species by chromatographic and electrophoretic methods. European Food Research and Technology 2005, 221, 542–546.
  • Nisbet, A.D.; Saundry, R.H.; Fothergill, L.A.; Fothergill, J.E. The complete amino-acid-sequence of hen ovalbumin. European Food Research and Technology 1981, 115, 335–345.
  • Ahmed, J.; Ramaswamy, H.S.; Alli, I.; Raghavan, G.S.V. Protein denaturation, rheology, and gelation characteristics of radio-frequency heated egg white dispersions. International Journal of Food Properties 2007, 10 (1),145–161.
  • Aoki, T.; Hiidome, Y.; Sugimoto, Y.; Ibrahim, H.R.; Kato, Y. Modification of ovalbumin with oligogalacturonic acids through the Maillard reaction. Food Research International 2001, 34, 127–132.
  • Hu, H.Y.; Du, H.N. Alpha-to-beta structural transformation of ovalbumin: Heat and pH effects. Journal of Protein Chemistry 2000, 19, 177–183.
  • Atlgan, M.R.; Unluturk, S. Rheological properties of liquid egg products (LEPS). International Journal of Food Properties 2008, 11, 296–309.
  • Huntington, J.A.; Stein, P.E. Structure and properties of ovalbumin. Journal of Chromatography B 2001, 756, 189–198.
  • Enomoto, H.; Nagae, S.; Hayashi, Y.; Li, C.P.; Ibrahim, H.R.; Sugimoto, Y.; Aoki, T. Improvement of functional properties of egg white protein through glycation and phosphorylation by dry-heating. Asian-Australasian Journal of Animal Sciences 2009, 22, 591–597.
  • Li, C.P.; Hayashi, Y.; Shinohara, H.; Ibrahim, H.R.; Sugimoto, Y.; Kurawaki, J.; Matsudomi, N.; Aoki, T. Phosphorylation of ovalbumin by dry-heating in the presence of pyrophosphate: Effect on protein structure and some properties. Journal of Agricultural and Food Chemistry 2005, 53, 4962–4967.
  • Oliveira, A.L.; Malafaya, P.B.; Costa, S.A.; Sousa, R.A.; Reis, R.L. Micro-computed tomography (mu-CT) as a potential tool to assess the effect of dynamic coating routes on the formation of biomimetic apatite layers on 3D-plotted biodegradable polymeric scaffolds. Journal of Materials Science–Materials in Medicine 2007, 18, 211–223.
  • Li, C.P.; Chen, D.; Peng, J.; Enomoto, H.; Hayashi, Y.; Li, C.; Ou, L.; Aoki, T. Improvement of functional properties of whey soy protein phosphorylated by dry-heating in the presence of pyrophosphate. LWT–Food Science and Technology 2010, 43, 919–925.
  • Hayakawa, S.; Nakai, S. Contribution of the hydrophobicity, net charge and sulfhydryl groups to thermal properties of ovalbumin. Candian Institute of Food Science and Technology 1985, 18, 290–295.
  • Lowry, O.H.; Rosebrough, N.J.; Farr, A.L.; Randall, R.J. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 1951, 193, 265–275.
  • Pearce, K.N.; Kinsella, J.E. Emulsifying properties of proteins: Evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry 1978, 26, 716–723.
  • Sosulski, F.W. The centrifuge method for determining flour absorption in hard red spring wheats. Cereal Chemistry 1962, 39, 344–350.
  • Zhang, X.C.; Tu, Z.C.; Zheng, W.W.; Li, P.; Chen, G.; Wang, H.; Dou, Y.X. Mechano-chemical effect on arachin by high pressure microfluidization. Acta Chimica Sinica 2009, 67, 2862–2866.
  • Batra, P.P.; Roebuck, M.A.; Uetrecht, D. Effect of lysine modification on the secondary structure of ovalbumin. Journal of Protein Chemistry 1990, 9, 37–44.
  • Benjamin, T.W.; Li, D.; Don, M.N.; Mary, A.A. The effect of maillard conjugation of deamidated wheat proteins with low molecular weight carbohydrateson the secondary structure of the protein. Food Biophysics 2009, 4, 1–12.
  • Nakai, S.; Li, C.E. Hydrophobicity-functionality relationship of food proteins. In: Hydrophobic Interactions in Food Systems; CRC Press: Boca Raton, FL, 1988; 47–48.
  • Fujiwara, K.; Oosawa, T.; Saeki, H. Improved thermal stability and emulsifying properties of carp myofibrillar proteins by conjugation with dextran. Journal of Agricultural and Food Chemistry 1998, 46, 1257–1261.
  • Kato, A.; Ibrahim, H.R.; Watanabe, H.; Honma, K.; Kobayashi, K. New approach to improve the gelling and surface functional-properties of dryed egg-white by heating in dry state. Journal of Agricultural and Food Chemistry 1989, 37, 433–437.

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