Changes of Physico-Chemical Properties of Whey Protein after Denaturation, Enzymatic Hydrolysis and Cross-Linking

Document Type : Research Paper

Authors

1 Assistant Professor, Department of Food Science and Engineering , Faculty of Agriculture, University of Kurdistan, Sanandaj, Iran

2 Professor, Department of Food Science and Engineering, Faculty of Agricultural engineering and Technology, College of Agriculture and Natural Resources, University of Tehran, Karaj, Iran

Abstract

In the current research, physico-chemical properties of whey protein isolate (WPI) and its resulting compounds including denatured whey protein isolate (DWPI), cross-linked whey protein isolate (CWPI), whey protein hydrolysate (WPH) and cross-linked whey protein hydrolysate (CWPH) were analyzed. Enzymatic hydrolysis and cross-linking were performed by pepsin (at 37°C for 30 min) and transglutaminase (at 50°C for 20 h), respectively. The obtained results stated that, by moderate heat, DWPI had smaller average size (44 nm) and more zeta-potential rather than native WPI. Intensity of the number of molecules with higher average particle size has been reduced by cross-linking of both DWPI and WPH using transglutaminase. Also, the antioxidant activity of WPH was increased from 0.398 to 0.519 through cross-linking and making larger peptide chain. The result of fourier-transform infrared spectroscopy (FTIR) indicated the enzymatic cross-linking owing to the formation of new C−N bonds between the α-carbon of lysine and the primary amine group of glutamine displaced the corresponding band at both CWPI and CWPH samples.

Keywords

Main Subjects

References

Adjonu, R., Doran, G., Torley, P. & Agboola, S. (2013). Screening of whey protein isolate hydrolysates for their dual functionality: influence of heat pre-treatment and enzyme specificity. Food Chemistry, 136, 1435‒1443.
Bagheri, L., Madadlou, A., Yarmand, M. & Mousavi, M. E. (2014). Potentially bioactive and caffeine‒loaded peptidic sub‒micron and nanoscalar particles. Journal of Functional Foods, 6, 462‒469.
Carvalho, N. C. D., Pessato, T. B., Negrão, F., Eberlin, M. N., Behrens, J. H., Zollner, R. D. L. & Netto, F. M. (2019). Physicochemical changes and bitterness of whey protein hydrolysates after transglutaminase cross-linking. LWT - Food Science and Technology, 113, 108291.
Chen, A., Tanidjaja, I. & Damodaran, S. (2018). Nanostructure and functionality of enzymatically repolymerized whey protein hydrolysate. Food Chemistry, 256, 405–412.
Damodaran, S. & Agyare, K. K. (2013). Effect of microbial transglutaminase treatment on thermal stability and pH-solubility of heat-shocked whey protein isolate. Food Hydrocolloids, 30, 12‒18.
Eissa, A. S., Bisram, S. & Khan, S. A. (2004). Polymerization and gelation of whey protein isolates at low pH using transglutaminase enzyme. Journal of Agricultural Food Chemistry, 52, 4456−4464.
Gaspar, L. & de Goes-Favoni, P. (2015). Action of microbial transglutaminase (MTGase) in the modification of food proteins : a review. Food Chemistry, 171, 315‒322.
Goudarzi, M., Madadlou, M., Mousavi, M. E. & Emam‐Djomeh, Z. (2015). Formulation of apple juice beverages containing whey protein isolate or whey protein hydrolysate based on sensory and physicochemical analysis. International Journal of Dairy Technology, 68, 70−78.
Gulseren, I., Fang, Y. & Corredig, M. (2012). Zinc incorporation capacity of whey protein nanoparticles prepared with desolvation with ethanol. Food Chemistry, 135, 770‒774.
Jiang, Z., Wang, C., Li, T., Sun, D., Gao, H. & Gao, Z. (2019). Effect of ultrasound on the structure and functional properties of transglutaminase-crosslinked whey protein isolate exposed to prior heat treatment. International Dairy Journal, 88, 79–88.
Kretschmer, C. B. (1957).Infrared spectroscopy and optical rotatory dispersion of zein, wheat gluten and gliadin. The Journal of Physical Chemistry, 61, 1627–1631.
Li, C., Zhang, D., Guo, H., Hao, L., Zheng, D., Liu, G., et al. (2013). Preparation and characterization of galactosylated bovine serum albumin nanoparticles for liver-targeted delivery of oridonin. International Journal of Pharmaceutics, 448, 79‒86.
Liu, G. & Zhong, Q. (2013). Dispersible and thermal stable nanofibrils derived from glycated whey protein. Biomacromolecules, 14, 2146−2153.
Madadlou, A. & Abbaspourrad. A. (2017). Bioactive whey peptide particles: An emerging class of nutraceutical carriers. Critical Review in Food Science and Nutrition, 58, 1468–1477.
Madadlou, A., Jaberipour, S. & Eskandari, M. H. (2014). Nanoparticulation of enzymatically cross-linked whey proteins to encapsulate caffeine via microemulsification/heat gelation procedure. LWT - Food Science and Technology, 57, 725–730.
Madureira, R., Tavares, T., Gomes, M., Pintado, E. & Malcata, X. (2010). Invited review: physiological properties of bioactive peptides obtained from whey proteins. Journal of Dairy Science, 93, 437–455.
Nielsen, P. M., Petersen, D. & Dambmann, C. (2001). Improved method for determining food protein degree of hydrolysis. Journal of Food Science, 66, 642–646.
Oanceaa, A., Hasanb, M., Vasilea, A. M., Barbua, V., Enachia, E. & et al. (2018). Functional evaluation of microencapsulated anthocyanins from sour cherries skins extract in whey proteins isolate. LWT - Food Science and Technology, 95, 129–134.
Shao, S., Shen, X. & Guo, M. (2018). Zinc‐loaded whey protein nanoparticles prepared by enzymatic cross‐linking and desolvation. International Journal of Food Science and Technology, 25, 1108-1120.
Tana, S., Zhonga, C. & Langrisha, T. (2019). Microencapsulation of pepsin in the spray-dried WPI (whey protein isolates) matrices for controlled release. Journal of Food Engineering, 263, 147–154.
Vahedifar, A., Madadlou, A. & Salami, M. (2018). Influence of seeding and stirring on the structural properties and formation yield of whey protein microgels. International Dairy Journal, 79, 43−51.
Van der Ven, C., Muresan, S., Gruppen, H., de Bont, D. B. A., Merck, K. B. & Voragen, A. G. J. (2002). FTIR Spectra of whey and casein hydrolysates in relation to their functional properties. Journal of Agricultural and Food Chemistry, 50, 6943‒6950.
Wang, W., Zhong, Q. & Hu, Z. (2013). Nanoscale understanding of thermal aggregation of whey protein pretreated by transglutaminase. Journal of Agricultural Food Chemistry, 61, 435−446.
Wu, C., Chen, M. & Shiau, Y. (2003). Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus). Food Research International, 36, 949–957.
Ye, Q., Woo, M .W. & Selomulya, C. (2019). Modification of molecular conformation of spray-dried whey protein microparticles improving digestibility and release characteristics. Food Chemistry, 280, 255–261.
Yildirim, A., Mavi, A. & Kara, A. A. (2001). Determination of antioxidant and antimicrobial activities of Rumex crispus L. extracts. Journal of Agricultural Food Chemistry, 49, 4083−4089.
Iranian Journal of Biosystems Engineering
Volume 50, Issue 4
January 2020
Pages 873-881

Files

History

  • Receive Date: 06 May 2019
  • Revise Date: 02 July 2019
  • Accept Date: 14 July 2019

Share

How to cite

Statistics