اثر واکنش میلارد بر خواص آنتی‌اکسیدانی و امولسیون کنندگی محصول هیدرولیز پروتئین عدس(Lens culinaris)
محورهای موضوعی : شیمی مواد غذاییصفا فرجی 1 , مهتا میرزایی 2 , سعید میردامادی 3
1 - دانشجوی کارشناسی ارشد، گروه علوم و صنایع غذایی، واحد شهر قدس، دانشگاه آزاد اسلامی، تهران، ایران
2 - استادیار گروه علوم و صنایع غذایی، واحد شهر قدس، دانشگاه آزاد اسلامی، تهران، ایران
3 - استاد پژوهشکده زیست فناوری، سازمان پژوهش‌های علمی و صنعتی ایران، تهران، ایران
کلید واژه: واکنش میلارد, هیدرولیز آنزیمی, امولسیون کنندگی, پروتئین عدس, فعالیت آنتی‌اکسیدانی,
چکیده مقاله :
مقدمه: محصولات هیدرولیز پروتئینی و پپتیدهای زیست فعال دارای اثرات سلامت بخش برای مصرف‌کنندگان هستند و واکنش گلیکوزیله شدن پروتئین‌ها یکی از روش‌های مورد توجه در بهبود خواص سلامت بخشی و عملکردی آنهاست. تاثیر دما، pH و نوع قند بر پیشرفت واکنش قهوه‌ای شدن محصول هیدرولیز پروتئین عدس و خواص آنتی‌اکسیدانی و امولسیون‌کنندگی آن موضوع این پژوهش بوده است. مواد و روش‌ها: پروتئین استخراج شده از دانه عدس تحت فرآیند هیدرولیز آنزیمی با آنزیم آلکالاز قرار گرفت و محصول هیدرولیز پروتئین به نسبت 1:1 با قندهای گلوکز و لاکتوز مخلوط و فرآیند میلارد در دماهای 60 و 80 درجه سانتی‌گراد و pHهای 5/6 و 11 انجام شد. پیشرفت واکنش میلارد در طی زمان با اندازه‌گیری شدت رنگ در طول موج ۴۲۰ نانومتر و میزان گروه‌های آمین آزاد با روش OPA اندازه‌گیری شد و فعالیت آنتی‌اکسیدانی محصول براساس مهارکنندگی رادیکال ABTS ارزیابی گردید. خواص امولسیون‌کنندگی محصول واکنش میلارد بر اساس اندازه‌گیری میزان جدب نور در نمونه آماده شده از ترکیب آن با روغن در طی زمان ارزیابی شد.یافته‌ها: نتایج نشان داد واکنش محصول هیدرولیز پروتئین عدس با قند گلوکز در دمای 60درجه سانتی‌گراد و pH5/6 باعث بیشترین شدت رنگ قهوه‌ای شده است و تغییر در میزان گروه‌های آمین آزاد نیز تایید کننده پیشرفت واکنش میلارد بود. با این وجود واکنش در شرایط دما و pH مشابه ولی درحضور قند لاکتوز با درجه قهوه‌ای شدن کمتر بیشترین تاثیر رادربهبود فعالیت آنتی‌اکسیدانی براساس مهار رادیکال ABTS داشت بطوریکه فعالیت آنتی‌اکسیدانی محصول هیدرولیز پروتئین عدس از 18/24 درصد به 97/60 درصد افزایش یافت و محصول تولیدی خاصیت امولسیون کنندگی بالاتری نسبت به نمونه کنترل داشت.نتیجه‌گیری: درمجموع نتایج نشان داد واکنش میلارد بین پروتئین‌ها و پپتیدهای موجود درمحصول هیدرولیز پروتئین عدس منجر به بهبود خواص سلامت بخشی و عملکردی آن می‌گردد و محصول تولیدی دارای پتانسیل کاربرددرفرمولاسیون محصولات غذایی فراسودمند است.
Introduction: Protein hydrolysates and bioactive peptides that have health benefits for consumers and protein glycolysis is a well-known strategy for increasing the health benefits and functional qualities of proteins. The subjects of this study were the effects of temperature, pH, and sugar type on the progress of the Mailard reaction in lentil protein hydrolysate, as well as its antioxidant and emulsification capabilities.Materials and Methods: The protein isolated from lentil seeds was hydrolyzed enzymatically by alkalase and mixed with glucose and lactose. Millard reaction occured at temperatures of 60 and 80 ° C and pHs of 6.5 and 11. The reaction progress was tracked over time by measuring the color intensity at 420 nm and the values of free amine groups using OPA method. The ABTS radical scavenging activity and emulsification capabilities of the final products product were analysed.Results: The results revealed that the reaction of lentil protein hydrolysate with glucose at 60 ° C and pH of 6.5 produced the most deep brown color. The findings of measuring the number of free amine groups also confirmed the results. Lactose sugar products with a lesser browning degree have the greatest effect on increasing antioxidant activity. Overall, the antioxidant activity of lentil protein hydrolyate increased from 24.18 to 60.97%, and its emulsifying function was enhanced.Conclusion: Overall, the results demonstrated that the Millard interaction between lentil protein hydrolysate proteins and peptides increases its health and functional qualities, and the product has the potential to be exploited in the formulation of functional foods.
Ames, J.M. (1998). Applications of the Maillard reaction in the food industry. Food Chemistry 62, 431-439.
Ajandouz, E. H., Tchiakpe, L. S., Ore, F. D., Benajiba, A. & Puigserver, A. (2001). Effects of pH on caramelization and Maillard reaction kinetics in fructose‐lysine model systems. Journal of Food Science, 66(7), 926-931.
Al-Hakkak, J. & Al-Hakkak, F. (2010). Functional egg white–pectin conjugates prepared by controlled Maillard reaction. Journal of Food Engineering, 100, 152-159.
Alizadeh, R., Mizraei, M . & Fadaei, V. (2020). Stability of antioxidant activity of lentil protein hydrolysis product against heat and pH treatments. Iranian Journal of Food Science and Technology Research, 5, 861-849 [In Persian].
Berlett, B.S. & Stadtman, E.R. (1997). Protein oxidation in aging, disease, and oxidative stress. Journal of Biological Chemistry, 272, 20313-20316.
Benjakul, S., Lertittikul, W. & Bauer, F. (2005). Antioxidant activity of Maillard reaction products from a porcine plasma protein–sugar model system. Food Chemistry, 93, 189-196.
Chang, H., Chen, Y. & Tan, F. (2011). Antioxidative properties of a chitosan–glucose Maillard reaction product and its effect on pork qualities during refrigerated storage. Food Chemistry, 124, 589-595.
Cumby, N., Zhong, Y., Naczk, M. & Shahidi, F. (2008). Antioxidant activity and water-holding capacity of canola protein hydrolysates. Food Chemistry, 109, 144-148.
Delgado-Andrade, C., Seiquer, I., Haro, A., Castellano, R. & Navarro, M.P. (2010). Development of the Maillard reaction in foods cooked by different techniques. Intake of Maillard-derived compounds. Food Chemistry, 122, 145-153.
Gheshlaghi Piri, S., Sadeghi Mahonak, A., Ghorbani, M. & Alami, M. (2018). Optimization of the process Optimization of the process of production of hydrolyzed protein from whey using alkalase enzyme. Journal of Food Science and Technology,77, 144-134 [In Persian].
Ghazanfarzadeh, Z. & Emami, L. (2014). Glycolysis is a promising method for modifying food proteins: a study of physicochemical properties and structure. National Conference on Meals, 1, 9-1 [In Persian].
Gu, F., Kim, J. M., Hayat, K., Xia, S., Feng, B. & Zhang, X. (2010). Characteristics and antioxidant activity of ultrafiltrated Maillard reaction products from a casein–glucose model system. Food Chemistry, 117(1), 48-54.
Ghasemi P, Mirzaei M. & Mirdamadi S. (2020). Effect of heat and freeze-thaw pretreatments on enzymatic hydrolysis of lentil protein by alkalase enzyme and production of antioxidant peptides. Journal of Food Science and Nutrition, 3, 32 -18 [In Persian].
Hoyle, N.T. & Merritt, J.H. (1994). Quality of fish protein hydrolysates from herring (Clupea harengus). Journal of food Science, 59, 76-79.
Hwang, I. G., Kim, H. Y., Woo, K. S., Lee, J. & Jeong, H. S. (2011). Biological activities of Maillard reaction products (MRPs) in a sugar–amino acid model system. Food Chemistry, 126(1), 221-227.
Hosseini, S., Ghareghi, A., Jamalzadeh, H., Safari, R. & Hosseini, S. (2013). Comparison of hydrolyzed protein from guts, viscera and head of phytophagous fish (Hypophthalmichthys molitrix) using alcalase enzyme and internal tissue enzymes. Scientific Journal of Fisheries, 3, 62-55 [In Persian].
Joshi, M., Timilsena, Y. & Adhikari, B. (2017). Global production, processing and utilization of lentil: A review. Journal of Integrative Agriculture, 16(12), 2898-2913.
Kim, J. S. & Lee, Y. S. (2009). Antioxidant activity of Maillard reaction products derived from aqueous glucose/glycine, diglycine, and triglycine model systems as a function of heating time. Food Chemistry, 116, 227-232.
Lowry, O., Rosebrough, N., Farr, A. & Randall, R. (1951). Total protein estimation by Lowry's method. The Journal of Biological Chemistry, 193(1), 265-275.
Li, Y., Lu, F., Luo, C., Chen, Z., Mao, J., Shoemaker, C. & Zhong, F. (2009). Functional properties of the Maillard reaction products of rice protein with sugar. Food Chemistry, 117, 69-74.
Liu, Q., Kong, B., Han, J., Sun, C. & Li, P. (2014). Structure and antioxidant activity of whey protein isolate conjugated with glucose via the Maillard reaction under dry-heating conditions. Food Structure, 1, 145-154.
Maqsoudlou, A., Mahoonak, A.S., Mora, L., Mohebodini, H., Toldrá, F. & Ghorbani, M. (2019). Peptide identification in alcalase hydrolysated pollen and comparison of its bioactivity with royal jelly. Food Research International, 116, 905-915.
Molaeifar, M., Larry, M., Mushri, M. & Bustani, S. (2017). The effect of microwave treatment on the rate of glycosylation of conjugates resulting from mylard lysozyme-maltodextrin reaction. Journal of Food Science and Technology, 60: 113- 105 [In Persian].
Maillard, M. N., Billaud, C., Chow, Y. N., Ordonaud, C. & Nicolas, J. (2007). Free radical scavenging, inhibition of polyphenoloxidase activity and copper chelating properties of model Maillard systems. LWT-Food Science and Technology, 40, 1434-1444.
Moscovici, A.M., Joubran, Y., Briard-Bion, V., Mackie, A., Dupont, D. & Lesmes, U. (2014). The impact of the Maillard reaction on the in vitro proteolytic breakdown of bovine lactoferrin in adults and infants. Food & Function, 5, 1898-1908.
Mengíbar, M., Miralles, B. & Heras, Á. (2017). Use of soluble chitosans in Maillard reaction products with β-lactoglobulin. Emulsifying and antioxidant properties. LWT, 75, 440-446.
Mirdamadi, S., Soliman Zadeh, N., Mirzaei, M. & Motahhari, P. (2017). Bioactive peptides: Production process, health effects and application as natural additives in the production of processed foods. Journal of Food Hygiene, 7(25), 1-20 [In Persian].
Mirzaei, M., Mirdamadi, S., Ehsani, M.R. & Aminlari, M. (2018). Production of antioxidant and ACE-inhibitory peptides from Kluyveromyces marxianus protein hydrolysates: Purification and molecular docking. Journal of Food and Drug Analysis, 26, 696-705.
Mokhtari, Sh. (2018). Antioxidant properties of Millard reaction products. 1-6 [In Persian].
Maqsoudlou, A., Mahoonak, A.S., Mora, L., Mohebodini, H., Toldrá, F. & Ghorbani, M. (2019). Peptide identification in alcalase hydrolysated pollen and comparison of its bioactivity with royal jelly. Food Research International, 116, 905-915.
Niki, E., Noguchi, N., Tsuchihashi, H. & Gotoh, N. (1995). Interaction among vitamin C, vitamin E, and beta-carotene. The American Journal of Clinical Nutrition, 62, 1322S-1326.
Nagpal, R., Behare, P., Rana, R., Kumar, A., Kumar, M., Arora, S., Morotta, F., Jain, S. & Yadav, H. (2011). Bioactive peptides derived from milk proteins and their health beneficial potentials: an update. Food & Function, 2, 18-27.
Nourmohammadi, A., Sadeghi Mahonak, A., Shahrampour, D. & Khamiri, M. ( 2015). Optimization of Hydrolysis of Pumpkin Seed Meal Protein Protein to Achieve Maximum Antioxidant Properties. Journal of Food Processing and Preservation, 9, 1-12 [In Persian].
Oseguera-Toledo, M.E., de Mejia, E.G., Dia, V.P. & Amaya-Llano, S.L. (2011). Common bean (Phaseolus vulgaris L.) hydrolysates inhibit inflammation in LPS-induced macrophages through suppression of NF-κB pathways. Food Chemistry, 127, 1175-1185.
Pownall, T.L., Udenigwe, C.C. & Aluko, R.E. (2010). Amino acid composition and antioxidant properties of pea seed (Pisum sativum L.) enzymatic protein hydrolysate fractions. Journal of agricultural and food chemistry 58, 4712-4718.
Re, R., Pellegrini, N., Proteggente, A., Pannala, A., Yang, M. & Rice-Evans, C. (1999). Antioxidant activity applying an improved ABTS radical cation decolorization assay. Free Radical Biology and Medicine, 26(9), 1231-1237.
Rajabzadeh, M., Pourashouri, P., Shabanpour, B. & Alishahi, A. (2018). Evaluation of functional and antioxidant properties of hydrolyzed rainbow trout egg protein (Oncorhyynchus mykiss) Journal of Innovation in Food Science and Technology, 10, 35-23 [In Persian].
Ranjbar Nedamani, E., Sadeghi Mahoonak, A., Ghorbani, M., Jacobsen, C. & Khouri, V. (2022). Improvement of antioxidant and emulsifying properties of Cajanus cajan’s protein hydrolysate by glycosylation through maillard reaction. Iranian Food Science and Technology Research Journal, 17(6), 137-152.
Su, G., Zheng, L., Cui, C., Yang, B., Ren, J. & Zhao, M. (2011). Characterization of antioxidant activity and volatile compounds of Maillard reaction products derived from different peptide fractions of peanut hydrolysate. Food Research International, 44, 3250-3258.
Shekaripour, F., Lari, M., Nia Kothari, M. & Eskandari, M. (2013). Investigating the effect of conjugation with dextran in Maillard reaction conditions on the functional and application properties of whey proteins. Journal of Innovation in Food Science and Technology, 5, 1-8 [In Persian].
Song, N., Tan, C., Huang, M., Liu, P., Eric, K., Zhang, X., Xia, S. & Jia, C. (2013). Transglutaminase cross-linking effect on sensory characteristics and antioxidant activities of Maillard reaction products from soybean protein hydrolysates. Food Chemistry, 136, 144-151.
Yilmaz, Y. & Toledo, R. (2005). Antioxidant activity of water-soluble Maillard reaction products. Food Chemistry, 93(2), 273-278.
Yavarnejad, N., Mirzaei, M. & Mirdamadi, S. (2019). Optimization of enzymatic hydrolysis parameters of lentil protein by response surface method with the aim of increasing antioxidant activity. International Congress on Agricultural Development, Natural Resources, Environment and Tourism of Iran, 1, 1-16 [In Persian].
_||_Ames, J.M. (1998). Applications of the Maillard reaction in the food industry. Food Chemistry 62, 431-439.
Ajandouz, E. H., Tchiakpe, L. S., Ore, F. D., Benajiba, A. & Puigserver, A. (2001). Effects of pH on caramelization and Maillard reaction kinetics in fructose‐lysine model systems. Journal of Food Science, 66(7), 926-931.
Al-Hakkak, J. & Al-Hakkak, F. (2010). Functional egg white–pectin conjugates prepared by controlled Maillard reaction. Journal of Food Engineering, 100, 152-159.
Alizadeh, R., Mizraei, M . & Fadaei, V. (2020). Stability of antioxidant activity of lentil protein hydrolysis product against heat and pH treatments. Iranian Journal of Food Science and Technology Research, 5, 861-849 [In Persian].
Berlett, B.S. & Stadtman, E.R. (1997). Protein oxidation in aging, disease, and oxidative stress. Journal of Biological Chemistry, 272, 20313-20316.
Benjakul, S., Lertittikul, W. & Bauer, F. (2005). Antioxidant activity of Maillard reaction products from a porcine plasma protein–sugar model system. Food Chemistry, 93, 189-196.
Chang, H., Chen, Y. & Tan, F. (2011). Antioxidative properties of a chitosan–glucose Maillard reaction product and its effect on pork qualities during refrigerated storage. Food Chemistry, 124, 589-595.
Cumby, N., Zhong, Y., Naczk, M. & Shahidi, F. (2008). Antioxidant activity and water-holding capacity of canola protein hydrolysates. Food Chemistry, 109, 144-148.
Delgado-Andrade, C., Seiquer, I., Haro, A., Castellano, R. & Navarro, M.P. (2010). Development of the Maillard reaction in foods cooked by different techniques. Intake of Maillard-derived compounds. Food Chemistry, 122, 145-153.
Gheshlaghi Piri, S., Sadeghi Mahonak, A., Ghorbani, M. & Alami, M. (2018). Optimization of the process Optimization of the process of production of hydrolyzed protein from whey using alkalase enzyme. Journal of Food Science and Technology,77, 144-134 [In Persian].
Ghazanfarzadeh, Z. & Emami, L. (2014). Glycolysis is a promising method for modifying food proteins: a study of physicochemical properties and structure. National Conference on Meals, 1, 9-1 [In Persian].
Gu, F., Kim, J. M., Hayat, K., Xia, S., Feng, B. & Zhang, X. (2010). Characteristics and antioxidant activity of ultrafiltrated Maillard reaction products from a casein–glucose model system. Food Chemistry, 117(1), 48-54.
Ghasemi P, Mirzaei M. & Mirdamadi S. (2020). Effect of heat and freeze-thaw pretreatments on enzymatic hydrolysis of lentil protein by alkalase enzyme and production of antioxidant peptides. Journal of Food Science and Nutrition, 3, 32 -18 [In Persian].
Hoyle, N.T. & Merritt, J.H. (1994). Quality of fish protein hydrolysates from herring (Clupea harengus). Journal of food Science, 59, 76-79.
Hwang, I. G., Kim, H. Y., Woo, K. S., Lee, J. & Jeong, H. S. (2011). Biological activities of Maillard reaction products (MRPs) in a sugar–amino acid model system. Food Chemistry, 126(1), 221-227.
Hosseini, S., Ghareghi, A., Jamalzadeh, H., Safari, R. & Hosseini, S. (2013). Comparison of hydrolyzed protein from guts, viscera and head of phytophagous fish (Hypophthalmichthys molitrix) using alcalase enzyme and internal tissue enzymes. Scientific Journal of Fisheries, 3, 62-55 [In Persian].
Joshi, M., Timilsena, Y. & Adhikari, B. (2017). Global production, processing and utilization of lentil: A review. Journal of Integrative Agriculture, 16(12), 2898-2913.
Kim, J. S. & Lee, Y. S. (2009). Antioxidant activity of Maillard reaction products derived from aqueous glucose/glycine, diglycine, and triglycine model systems as a function of heating time. Food Chemistry, 116, 227-232.
Lowry, O., Rosebrough, N., Farr, A. & Randall, R. (1951). Total protein estimation by Lowry's method. The Journal of Biological Chemistry, 193(1), 265-275.
Li, Y., Lu, F., Luo, C., Chen, Z., Mao, J., Shoemaker, C. & Zhong, F. (2009). Functional properties of the Maillard reaction products of rice protein with sugar. Food Chemistry, 117, 69-74.
Liu, Q., Kong, B., Han, J., Sun, C. & Li, P. (2014). Structure and antioxidant activity of whey protein isolate conjugated with glucose via the Maillard reaction under dry-heating conditions. Food Structure, 1, 145-154.
Maqsoudlou, A., Mahoonak, A.S., Mora, L., Mohebodini, H., Toldrá, F. & Ghorbani, M. (2019). Peptide identification in alcalase hydrolysated pollen and comparison of its bioactivity with royal jelly. Food Research International, 116, 905-915.
Molaeifar, M., Larry, M., Mushri, M. & Bustani, S. (2017). The effect of microwave treatment on the rate of glycosylation of conjugates resulting from mylard lysozyme-maltodextrin reaction. Journal of Food Science and Technology, 60: 113- 105 [In Persian].
Maillard, M. N., Billaud, C., Chow, Y. N., Ordonaud, C. & Nicolas, J. (2007). Free radical scavenging, inhibition of polyphenoloxidase activity and copper chelating properties of model Maillard systems. LWT-Food Science and Technology, 40, 1434-1444.
Moscovici, A.M., Joubran, Y., Briard-Bion, V., Mackie, A., Dupont, D. & Lesmes, U. (2014). The impact of the Maillard reaction on the in vitro proteolytic breakdown of bovine lactoferrin in adults and infants. Food & Function, 5, 1898-1908.
Mengíbar, M., Miralles, B. & Heras, Á. (2017). Use of soluble chitosans in Maillard reaction products with β-lactoglobulin. Emulsifying and antioxidant properties. LWT, 75, 440-446.
Mirdamadi, S., Soliman Zadeh, N., Mirzaei, M. & Motahhari, P. (2017). Bioactive peptides: Production process, health effects and application as natural additives in the production of processed foods. Journal of Food Hygiene, 7(25), 1-20 [In Persian].
Mirzaei, M., Mirdamadi, S., Ehsani, M.R. & Aminlari, M. (2018). Production of antioxidant and ACE-inhibitory peptides from Kluyveromyces marxianus protein hydrolysates: Purification and molecular docking. Journal of Food and Drug Analysis, 26, 696-705.
Mokhtari, Sh. (2018). Antioxidant properties of Millard reaction products. 1-6 [In Persian].
Maqsoudlou, A., Mahoonak, A.S., Mora, L., Mohebodini, H., Toldrá, F. & Ghorbani, M. (2019). Peptide identification in alcalase hydrolysated pollen and comparison of its bioactivity with royal jelly. Food Research International, 116, 905-915.
Niki, E., Noguchi, N., Tsuchihashi, H. & Gotoh, N. (1995). Interaction among vitamin C, vitamin E, and beta-carotene. The American Journal of Clinical Nutrition, 62, 1322S-1326.
Nagpal, R., Behare, P., Rana, R., Kumar, A., Kumar, M., Arora, S., Morotta, F., Jain, S. & Yadav, H. (2011). Bioactive peptides derived from milk proteins and their health beneficial potentials: an update. Food & Function, 2, 18-27.
Nourmohammadi, A., Sadeghi Mahonak, A., Shahrampour, D. & Khamiri, M. ( 2015). Optimization of Hydrolysis of Pumpkin Seed Meal Protein Protein to Achieve Maximum Antioxidant Properties. Journal of Food Processing and Preservation, 9, 1-12 [In Persian].
Oseguera-Toledo, M.E., de Mejia, E.G., Dia, V.P. & Amaya-Llano, S.L. (2011). Common bean (Phaseolus vulgaris L.) hydrolysates inhibit inflammation in LPS-induced macrophages through suppression of NF-κB pathways. Food Chemistry, 127, 1175-1185.
Pownall, T.L., Udenigwe, C.C. & Aluko, R.E. (2010). Amino acid composition and antioxidant properties of pea seed (Pisum sativum L.) enzymatic protein hydrolysate fractions. Journal of agricultural and food chemistry 58, 4712-4718.
Re, R., Pellegrini, N., Proteggente, A., Pannala, A., Yang, M. & Rice-Evans, C. (1999). Antioxidant activity applying an improved ABTS radical cation decolorization assay. Free Radical Biology and Medicine, 26(9), 1231-1237.
Rajabzadeh, M., Pourashouri, P., Shabanpour, B. & Alishahi, A. (2018). Evaluation of functional and antioxidant properties of hydrolyzed rainbow trout egg protein (Oncorhyynchus mykiss) Journal of Innovation in Food Science and Technology, 10, 35-23 [In Persian].
Ranjbar Nedamani, E., Sadeghi Mahoonak, A., Ghorbani, M., Jacobsen, C. & Khouri, V. (2022). Improvement of antioxidant and emulsifying properties of Cajanus cajan’s protein hydrolysate by glycosylation through maillard reaction. Iranian Food Science and Technology Research Journal, 17(6), 137-152.
Su, G., Zheng, L., Cui, C., Yang, B., Ren, J. & Zhao, M. (2011). Characterization of antioxidant activity and volatile compounds of Maillard reaction products derived from different peptide fractions of peanut hydrolysate. Food Research International, 44, 3250-3258.
Shekaripour, F., Lari, M., Nia Kothari, M. & Eskandari, M. (2013). Investigating the effect of conjugation with dextran in Maillard reaction conditions on the functional and application properties of whey proteins. Journal of Innovation in Food Science and Technology, 5, 1-8 [In Persian].
Song, N., Tan, C., Huang, M., Liu, P., Eric, K., Zhang, X., Xia, S. & Jia, C. (2013). Transglutaminase cross-linking effect on sensory characteristics and antioxidant activities of Maillard reaction products from soybean protein hydrolysates. Food Chemistry, 136, 144-151.
Yilmaz, Y. & Toledo, R. (2005). Antioxidant activity of water-soluble Maillard reaction products. Food Chemistry, 93(2), 273-278.
Yavarnejad, N., Mirzaei, M. & Mirdamadi, S. (2019). Optimization of enzymatic hydrolysis parameters of lentil protein by response surface method with the aim of increasing antioxidant activity. International Congress on Agricultural Development, Natural Resources, Environment and Tourism of Iran, 1, 1-16 [In Persian].
