คุณสมบัติทางเคมีกายภาพโปรตีนไข่ขาวไฮโดรไลเซตแห้งแช่เยือกแข็งที่ย่อยด้วยเอนไซม์นิวเทรส
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ม.ค. 30, 2020
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โปรตีนไข่ขาวไฮโดรไลเชต นิวเทรส การกระจายตัวของขนาดโมเลกุล การเกิดโฟม อิมัลซิไฟเออร์
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บทคัดย่อ
การคัดเลือกโปรตีนไข่ขาวไฮโดรไลเชตไปประยุกต์ใช้ในอุตสาหกรรมอาหารนั้น สมบัติทางเคมีกายภาพด้านอุณหภูมิและค่า pH ส่งผลต่อสมบัติเชิงหน้าที่ทางด้านความสามารถในการละลาย การเกิดโฟม และอิมัลซิไฟเออร์ ถือว่าเป็นปัจจัยสำคัญในการคัดเลือกไปใช้ในอุตสาหกรรม การวิจัยนี้เพื่อศึกษาผลของการย่อยสลายโปรตีนไข่ขาวด้วยเอนไซม์นิวเทรสที่ความเข้มข้นเอมไซม์ร้อยละ 1 (v/v) ที่อุณหภูมิ 45, 50 และ 55 องศาเซลเซียส และ pH 5, 6 และ 7 ในช่วงระยะเวลา 30 นาที ถึง 6 ชั่วโมงผลการศึกษาพบว่าเอนไซม์นิวเทรสสามารถย่อยสลายเพิ่มขึ้นเมื่อระยะเวลาเพิ่มขึ้นโดยมีระดับการย่อยสลายเหมาะสมสูงสุดเท่ากับ 51 เปอร์เซ็นต์ ที่อุณหภูมิ 50 องศาเซลเซียส และ pH 7.0 ซึ่งระดับการย่อยสลายขึ้นอยู่กับความเป็นกรด-ด่าง อุณหภูมิและระยะเวลาของการย่อยสลายอย่างมีนัยสำคัญ การวิเคราะห์การกระจายน้ำหนักโมเลกุลของโปรตีนไฮโดรไลเชตในช่วง 1–100 กิโลดาลตัน พบว่ามีสัดส่วนของโปรตีนขนาดเล็กสูงกว่าโปรตีนไข่ขาวที่ไม่ผ่านการย่อยสลายด้วยเอนไซม์ มีสัดส่วนขนาด 30–100, 10–30, 5–10, 3–5, 1–3 และน้อยกว่า 1 กิโลดาลตัน 11.60, 9.90, 12.04, 8.54 และ 8.81 เปอร์เซ็นต์ ตามลำดับการศึกษาสมบัติการละลาย การเกิดโฟม ความเสถียรของโฟม และอิมัลซิไฟเออร์ที่ระดับ pH 3.6, 7.6 และ 9.0 ของโปรตีนไข่ขาวไฮโดรไลเซตด้วยเอนไซม์นิวเทรสที่อุณหภูมิ 50 องศาเซลเซียส pH 7 ที่ผ่านการทำแห้งแบบแช่เยือกแข็ง พบว่าสมบัติในการเกิดโฟม ความเสถียรของโฟม และสมบัติอิมัลซิไฟเออร์ขึ้นอยู่กับค่าความเป็นกรด-ด่าง โปรตีนไข่ขาวไฮโดรไลเซตที่มีโปรตีนขนาดเล็กเพิ่มขึ้นส่งผลให้ความสามารถในการละลายและเกิดโฟมเพิ่มขึ้น แต่ความสามารถในการเป็นอิมัลซิไฟเออร์ลดลง
Article Details
บท
บทความวิจัย ด้านวิทยาศาสตร์ประยุกต์
บทความที่ลงตีพิมพ์เป็นข้อคิดเห็นของผู้เขียนเท่านั้น
ผู้เขียนจะต้องเป็นผู้รับผิดชอบต่อผลทางกฎหมายใดๆ ที่อาจเกิดขึ้นจากบทความนั้น
References
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[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.