Physicochemical Characteristics of Freeze Dried Egg White Protein Hydrolyzed by Neutrase
Article Sidebar
Published:
Jan 30, 2020
Keywords:
Egg White Protein Hydrolysate Neutrase Molecular Distribution Foaming Emulsifying Properties
Main Article Content
Abstract
The effects of temperature and pH on the physicochemical attributes as solubility, foaming and emulsifying properties of egg white protein hydrolysate are important functional quantities for selecting applications in food industries. In this research, 1% (v/v) Neutrase was used to hydrolyze egg white protein under various temperatures (45, 50 and 55°C) and pHs (5, 6 and 7) over increasing hydrolysis times (30 min to 6 hours). The effects of Neutrase hydrolysis showed that degree of hydrolysis (DH) increased with increasing hydrolysis times resulting in 51% DH at the optimum temperature of 50°C, pH 7.0. Significantly differences of DH were detected in different pH levels, temperatures and hydrolysis times. The molecular distributions of protein hydrolysate in the ranges of 1–100 kDa at optimum hydrolysis condition were reported. Result showed the smaller size proteins in range of 30–100, 10–30, 5–10, 3–5, 1–3 and <1 kDa of 11.60, 9.90, 12.04, 8.54 and 8.81%, respectively. The freeze dried yield of egg white protein hydrolysate at 50°C, pH 7.0 was further investigated for solubility in pH values, 3.6, 7.6 and 9.0 with the foaming capacity and stability associated to those pH values. The emulsifying activity index of various pHs was also explained. These results indicated that the foaming of egg white hydrolysate increased as increasing solubility; however, emulsifying properties were decreased as decreasing solubility.
Article Details
Section
Applied Science Research Articles
The articles published are the opinion of the author only. The author is responsible for any legal consequences. That may arise from that article.
References
[1] C. Chen and Y. J. Chi, “Antioxidant, ACE inhibitory activities and functional properties of egg white protein hydrolysate,” Journal of Food Biochemistry, vol. 36, no. 4, pp. 383–394, 2012.
[2] D. Lunow, S. Kaiser, S. Bruckner, A. Gotsch, and T. Henle, “Selective release of ACE-inhibiting tryptophan-containing dipeptides from food proteins by enzymatic hydrolysis,” European Food Research and Technology, vol. 237, no. 1, pp. 27–37, 2013.
[3] E. Eckert, A. Zambrowicz, M. Pokora, A. Polanowski, J. Chrzanowska, M. Szoltysik, A. Dabrowska, H. Róz˙an´ski, and T. Trziska, “Biologically active peptides derived from egg proteins,” World’s Poultry Science Journal, vol. 69, no. 2, pp. 375–386, 2013.
[4] A. Singh and HS. Ramaswamy, “Effect of highpressure treatment on trypsin hydrolysis and antioxidant activity of egg white proteins,” International Journal of Food Science & Technology, vol. 49, no. 1, pp. 269–279, 2014.
[5] S. Lin, Y. Jin, M. Liu, Y. Yang, M. Zhang, Y. Guo, G. Jones, J. Liu, and Y. Yin, “Research on the preparation of antioxidant peptides derived from egg white with assisting of high-intensity pulsed electric field,” Food Chem, vol. 139, no. 1–4, pp. 300–306, 2013.
[6] N. J. Adamson and E. C. Reynolds, “Characterization of casein phosphopeptides prepared alcalase: Determination of enzyme specificity,” Enzyme and Microbial Technology, vol. 19, no. 3, pp. 202–207, 1996.
[7] X. Ren, H. Ma, S. Mao, and H. Zhou, “Effects of sweeping frequency ultrasound treatment on enzymatic preparations of ACE inhibitory peptides from zein,” European Food Research and Technology, vol. 238, no. 3, pp. 435–442, 2014.
[8] D. Y. Cho, K. Jo, S. Y. Cho, J. M. Kim, K. Lim, H. J. Suh, and S. Oh, “Antioxidant effect and functional properties of hydrolysates derived from egg-white protein,” Korean Journal for Food Science of Animal Resources, vol. 34, no. 3, pp. 362–371, 2014.
[9] K. Venkatachalam and M. Nagarajan. “Assessment of different proteases on degree of hydrolysis, functional properties and radical scavenging activities of salted duck egg white hydrolysate” Journal of Food Science and Technology, vol. 56, no. 6, pp. 3137–3144. 2019.
[10] D. Panyam and A. Kilara, “Enhancing the functionality of food proteins by enzymatic modification,” Trends in Food Science & Technology, vol. 7, no. 4, pp. 120–125, 1996.
[11] R. Nagpal, P. Behare, R. Rana, A. Kumar, M. Kumar, S. Arora, and H. Yadav, “Bioactive peptides derived from milk proteins and their health beneficial potentials: An update,” Food & Function, vol. 2, no. 1, pp. 18–27, 2011.
[12] Z. F. Bhat, S. Kumar, and H. F. Bhat, “Bioactive peptides from egg: A review,” Nutrition & Food Science, vol. 45, no. 2, pp. 190–212, 2015.
[13] T. Lafarga and M. Hayes, “Bioactive peptides from meat muscle and by-products: Generation, functionality and application as functional ingredients,” Meat Science, vol. 98, no. 2, pp. 227–239, 2014.
[14] P. A. Harnedy and R. J. FitzGerald, “Bioactive peptides from marine processing waste and shellfish: A review,” Journal of Functional Foods, vol. 4, no. 1, pp. 6–24, 2012.
[15] Official Methods of Analysis of the Association of Official Analytical Chemists, 17th ed. Washington, D.C. 2000.
[16] S. Benjakul and M. T. Morrissey, “Protein hydrolysates from Pacific whiting solid wastes,” Journal of Agricultural & Food Chemistry, vol. 45, no. 9, pp. 3423–3430, 1997.
[17] C. V. Morr, “Composition, physico-chemical and functional properties of reference whey protein concentrates,” Journal of Food Science, vol. 50, no. 5, pp. 1406–1411, 1985.
[18] S. Sathe and D. Salunkhe, “Functional properties of the great northern bean (Phaseolus vulgaris L.) proteins: Emulsion, foaming, viscosity, and gelation properties,” Journal of Food Science, vol. 46, no. 6, pp. 71–81, 1981.
[19] K. N. Pearce and J. E. Kinsella, “Emulsifying properties of proteins: Evaluation of a turbidimetric technique,” Journal of Agricultural and Food Chemistry, vol. 26, pp. 716–723, 1978.
[20] M. Ai, T. Tang, L. Zhou, Z. Ling, and S. Guo, “Effects of different proteases on the emulsifying capacity, rheological and structure characteristics of preserved egg white hydrolysates,” Food Hydrocolloids, vol. 87, pp. 933–942, 2019.
[21] S. J. Ge and L. X. Zhang, “Control of hydrolysis of a protein modification with immobilized protease by the pH-drop method,” Acta Biotechnol, vol. 13, no. 2, pp. 151–160, 1993.
[22] A. Graszkiewicz, M. elazko, T. Trziszka, and A. Polanowski, “Antioxidative capacity of hydrolysates of hen egg proteins,” Polish Journal of Food and Nutrition Sciences, vol. 57, no. 4, pp. 195–199, 2007.
[23] A. Graszkiewicz, M. elazko, and T. Trziszka, “Application of pancreatic enzymes in hydrolysis of egg-white proteins,” Polish Journal of Food and Nutrition Sciences, vol. 60, no. 1, pp. 57–61, 2010.
[24] H. G. Kristinsson and B. A. Rasco, “Fish protein hydrolysates: Production, biochemical, and functional properties,” Critical Reviews in Food Science and Nutrition, vol. 40, no. 1, pp. 43–81, 2000.
[25] J. A. Huntington and P. E. Stein, “Structure and properties of ovalbumin,” Journal of chromatography, Biomedical sciences and applications, vol. 756, no. 1–2, pp. 189–198. 2001.
[26] W. J. Stadelman and O. J. Cotterill, Egg Science and Technology, 4th ed. Westport, CT, USA: Avi Publ. Co., 2001.
[27] R. Huopalahti, R. L. Fandino, M. Anton, and R. Ed. Schade, Bioactive Egg Compounds, New York, NY, USA: Springer, 2007.
[28] D. A. Oman, J. Wang, and J. Wu, “Co-extraction of egg white proteins using ion-exchange chromatography from ovomucin-removed egg white,” Journal of Chromatography B, vol. 878, no. 21, pp. 1771–1776, 2010.
[29] F. C. Oliveira, J. S. R. Coimbra, L. H. M. Silva, E. E. G. Rojas, and M. C. H. Silva, “Ovomucoid partitioning in aqueous two-phase system,” Biochemical Engineering Journal, vol. 47, no. 1–3, pp. 55–60, 2009.
[30] O. L. Tavano, “Protein hydrolysis using proteases: An important tool for food biotechnology,” Journal of Molecular Catalysis B Enzymatic, vol. 90, pp. 1–11, 2013.
[31] N. Charoenphun, W. Youravong, and B. Cheirsilp, “Determination of reaction kinetics of hydrolysis of tilapia (Oreochromis niloticus) protein for manipulating production of bioactive peptides with antioxidant activity, angiotensin-I-converting enzyme inhibitory activity and Ca-binding properties,” International Journal of Food Science & amp; Technology, vol. 48, no. 2, pp. 419–428, 2013.
[32] A. Davalõs, M. Miguel, B. Bartolome, and R. Lopez-Fandino, “Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis,” Journal of Food Protection, vol. 67, no. 9, pp. 1939–1944, 2004.
[33] W. Chiang, M. Lee, W. Guo, and T. Tsai. “Protein hydrolysates batch production with angiotensin I–converting enzyme inhibitory activity from egg whites,” Journal of Food and Drug Analysis, vol. 14, no. 4, pp. 385–390, 2006.
[34] M. Miguel and A. Aleixandre, “Antihypertensive peptides derived from egg proteins,” Journal of Nutrition, vol. 136, no. 6, pp. 1457–1460, 2006.
[35] H. Fujita, K. Yokoyama, and M. Yoshikawa. “Classification and antihypertensive activity of Angiotensin I–converting enzyme inhibitory peptides derived from food proteins,” Journal of Food Science, vol. 65, no. 4, pp. 564–569, 2000.
[36] M. A. Manso, M. Miguel, J. Even, R. Hernandez, A. Aleixandre, and R. Lopez-Fandino, “Effect of the long-term intake of egg white hydrolysates on the oxidative status and blood lipid profile of spontaneously hypertensive rats,” Food Chem, vol. 109, no. 2, pp. 361–367, 2008.
[37] Q. Liu, B. Kong, Y. L. Xiong, and X. Xia, “Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis,” Food Chem, vol. 118, no. 2, pp. 403–410, 2010.
[38] E. A. Foegeding, P. J. Luck, and J. P. Davis, “Factors determining the physical properties of protein foams,” Food Hydrocolloids, vol. 20, no. 2, pp. 284–292, 2006.
[2] D. Lunow, S. Kaiser, S. Bruckner, A. Gotsch, and T. Henle, “Selective release of ACE-inhibiting tryptophan-containing dipeptides from food proteins by enzymatic hydrolysis,” European Food Research and Technology, vol. 237, no. 1, pp. 27–37, 2013.
[3] E. Eckert, A. Zambrowicz, M. Pokora, A. Polanowski, J. Chrzanowska, M. Szoltysik, A. Dabrowska, H. Róz˙an´ski, and T. Trziska, “Biologically active peptides derived from egg proteins,” World’s Poultry Science Journal, vol. 69, no. 2, pp. 375–386, 2013.
[4] A. Singh and HS. Ramaswamy, “Effect of highpressure treatment on trypsin hydrolysis and antioxidant activity of egg white proteins,” International Journal of Food Science & Technology, vol. 49, no. 1, pp. 269–279, 2014.
[5] S. Lin, Y. Jin, M. Liu, Y. Yang, M. Zhang, Y. Guo, G. Jones, J. Liu, and Y. Yin, “Research on the preparation of antioxidant peptides derived from egg white with assisting of high-intensity pulsed electric field,” Food Chem, vol. 139, no. 1–4, pp. 300–306, 2013.
[6] N. J. Adamson and E. C. Reynolds, “Characterization of casein phosphopeptides prepared alcalase: Determination of enzyme specificity,” Enzyme and Microbial Technology, vol. 19, no. 3, pp. 202–207, 1996.
[7] X. Ren, H. Ma, S. Mao, and H. Zhou, “Effects of sweeping frequency ultrasound treatment on enzymatic preparations of ACE inhibitory peptides from zein,” European Food Research and Technology, vol. 238, no. 3, pp. 435–442, 2014.
[8] D. Y. Cho, K. Jo, S. Y. Cho, J. M. Kim, K. Lim, H. J. Suh, and S. Oh, “Antioxidant effect and functional properties of hydrolysates derived from egg-white protein,” Korean Journal for Food Science of Animal Resources, vol. 34, no. 3, pp. 362–371, 2014.
[9] K. Venkatachalam and M. Nagarajan. “Assessment of different proteases on degree of hydrolysis, functional properties and radical scavenging activities of salted duck egg white hydrolysate” Journal of Food Science and Technology, vol. 56, no. 6, pp. 3137–3144. 2019.
[10] D. Panyam and A. Kilara, “Enhancing the functionality of food proteins by enzymatic modification,” Trends in Food Science & Technology, vol. 7, no. 4, pp. 120–125, 1996.
[11] R. Nagpal, P. Behare, R. Rana, A. Kumar, M. Kumar, S. Arora, and H. Yadav, “Bioactive peptides derived from milk proteins and their health beneficial potentials: An update,” Food & Function, vol. 2, no. 1, pp. 18–27, 2011.
[12] Z. F. Bhat, S. Kumar, and H. F. Bhat, “Bioactive peptides from egg: A review,” Nutrition & Food Science, vol. 45, no. 2, pp. 190–212, 2015.
[13] T. Lafarga and M. Hayes, “Bioactive peptides from meat muscle and by-products: Generation, functionality and application as functional ingredients,” Meat Science, vol. 98, no. 2, pp. 227–239, 2014.
[14] P. A. Harnedy and R. J. FitzGerald, “Bioactive peptides from marine processing waste and shellfish: A review,” Journal of Functional Foods, vol. 4, no. 1, pp. 6–24, 2012.
[15] Official Methods of Analysis of the Association of Official Analytical Chemists, 17th ed. Washington, D.C. 2000.
[16] S. Benjakul and M. T. Morrissey, “Protein hydrolysates from Pacific whiting solid wastes,” Journal of Agricultural & Food Chemistry, vol. 45, no. 9, pp. 3423–3430, 1997.
[17] C. V. Morr, “Composition, physico-chemical and functional properties of reference whey protein concentrates,” Journal of Food Science, vol. 50, no. 5, pp. 1406–1411, 1985.
[18] S. Sathe and D. Salunkhe, “Functional properties of the great northern bean (Phaseolus vulgaris L.) proteins: Emulsion, foaming, viscosity, and gelation properties,” Journal of Food Science, vol. 46, no. 6, pp. 71–81, 1981.
[19] K. N. Pearce and J. E. Kinsella, “Emulsifying properties of proteins: Evaluation of a turbidimetric technique,” Journal of Agricultural and Food Chemistry, vol. 26, pp. 716–723, 1978.
[20] M. Ai, T. Tang, L. Zhou, Z. Ling, and S. Guo, “Effects of different proteases on the emulsifying capacity, rheological and structure characteristics of preserved egg white hydrolysates,” Food Hydrocolloids, vol. 87, pp. 933–942, 2019.
[21] S. J. Ge and L. X. Zhang, “Control of hydrolysis of a protein modification with immobilized protease by the pH-drop method,” Acta Biotechnol, vol. 13, no. 2, pp. 151–160, 1993.
[22] A. Graszkiewicz, M. elazko, T. Trziszka, and A. Polanowski, “Antioxidative capacity of hydrolysates of hen egg proteins,” Polish Journal of Food and Nutrition Sciences, vol. 57, no. 4, pp. 195–199, 2007.
[23] A. Graszkiewicz, M. elazko, and T. Trziszka, “Application of pancreatic enzymes in hydrolysis of egg-white proteins,” Polish Journal of Food and Nutrition Sciences, vol. 60, no. 1, pp. 57–61, 2010.
[24] H. G. Kristinsson and B. A. Rasco, “Fish protein hydrolysates: Production, biochemical, and functional properties,” Critical Reviews in Food Science and Nutrition, vol. 40, no. 1, pp. 43–81, 2000.
[25] J. A. Huntington and P. E. Stein, “Structure and properties of ovalbumin,” Journal of chromatography, Biomedical sciences and applications, vol. 756, no. 1–2, pp. 189–198. 2001.
[26] W. J. Stadelman and O. J. Cotterill, Egg Science and Technology, 4th ed. Westport, CT, USA: Avi Publ. Co., 2001.
[27] R. Huopalahti, R. L. Fandino, M. Anton, and R. Ed. Schade, Bioactive Egg Compounds, New York, NY, USA: Springer, 2007.
[28] D. A. Oman, J. Wang, and J. Wu, “Co-extraction of egg white proteins using ion-exchange chromatography from ovomucin-removed egg white,” Journal of Chromatography B, vol. 878, no. 21, pp. 1771–1776, 2010.
[29] F. C. Oliveira, J. S. R. Coimbra, L. H. M. Silva, E. E. G. Rojas, and M. C. H. Silva, “Ovomucoid partitioning in aqueous two-phase system,” Biochemical Engineering Journal, vol. 47, no. 1–3, pp. 55–60, 2009.
[30] O. L. Tavano, “Protein hydrolysis using proteases: An important tool for food biotechnology,” Journal of Molecular Catalysis B Enzymatic, vol. 90, pp. 1–11, 2013.
[31] N. Charoenphun, W. Youravong, and B. Cheirsilp, “Determination of reaction kinetics of hydrolysis of tilapia (Oreochromis niloticus) protein for manipulating production of bioactive peptides with antioxidant activity, angiotensin-I-converting enzyme inhibitory activity and Ca-binding properties,” International Journal of Food Science & amp; Technology, vol. 48, no. 2, pp. 419–428, 2013.
[32] A. Davalõs, M. Miguel, B. Bartolome, and R. Lopez-Fandino, “Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis,” Journal of Food Protection, vol. 67, no. 9, pp. 1939–1944, 2004.
[33] W. Chiang, M. Lee, W. Guo, and T. Tsai. “Protein hydrolysates batch production with angiotensin I–converting enzyme inhibitory activity from egg whites,” Journal of Food and Drug Analysis, vol. 14, no. 4, pp. 385–390, 2006.
[34] M. Miguel and A. Aleixandre, “Antihypertensive peptides derived from egg proteins,” Journal of Nutrition, vol. 136, no. 6, pp. 1457–1460, 2006.
[35] H. Fujita, K. Yokoyama, and M. Yoshikawa. “Classification and antihypertensive activity of Angiotensin I–converting enzyme inhibitory peptides derived from food proteins,” Journal of Food Science, vol. 65, no. 4, pp. 564–569, 2000.
[36] M. A. Manso, M. Miguel, J. Even, R. Hernandez, A. Aleixandre, and R. Lopez-Fandino, “Effect of the long-term intake of egg white hydrolysates on the oxidative status and blood lipid profile of spontaneously hypertensive rats,” Food Chem, vol. 109, no. 2, pp. 361–367, 2008.
[37] Q. Liu, B. Kong, Y. L. Xiong, and X. Xia, “Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis,” Food Chem, vol. 118, no. 2, pp. 403–410, 2010.
[38] E. A. Foegeding, P. J. Luck, and J. P. Davis, “Factors determining the physical properties of protein foams,” Food Hydrocolloids, vol. 20, no. 2, pp. 284–292, 2006.
