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نوع مقاله: مقاله کامل پژوهشی


1 دانشجوی کارشناسی ارشد، گروه علوم و صنایع غذایی، دانشگاه علوم کشاورزی و منابع طبیعی گرگان، گرگان، ایران

2 دانشیار، گروه علوم و صنایع غذایی، دانشگاه علوم کشاورزی و منابع طبیعی گرگان، گرگان، ایران

3 استادیار، گروه علوم و صنایع غذایی، دانشگاه علوم کشاورزی و منابع طبیعی گرگان، گرگان، ایران

4 استاد، گروه علوم و صنایع غذایی، دانشگاه علوم کشاورزی و منابع طبیعی گرگان، گرگان، ایران


در این پژوهش، بهینه‌سازی شرایط هیدرولیز پروتئین دانۀ کدو (Cucurbita pepo) به‌منظور دستیابی به حداکثر خصوصیات مهارکنندگی رادیکال 2،2- دی فنیل -1-پیکریل هیدرازیل (DPPH) و مهارکنندگی اکسید نیتریک با استفاده از نرم‌افزار Design Expert و روش سطح پاسخ موردبررسی قرار گرفت. به‌این‌منظور غلظت آنزیم آلکالاز 0/7-3/30 درصد، دمای 32-58 درجۀ‌ سانتی‌گراد و زمان 30-290 دقیقه به‌عنوان سطوح متغیرهای مستقل انتخاب شدند. نتایج نشان داد که شرایط بهینه برای دستیابی به حداکثر خاصیت مهارکنندگی رادیکال DPPH و مهارکنندگی اکسید نیتریک، دمای 44 درجۀ سانتی‌گراد، زمان 260 دقیقه و غلظت آنزیم به سوبسترا 3 درصد و با قابلیت ضداکسایشی و مهارکنندگی اکسید نیتریک برابر با 72/03 و 89/34 درصد بود که تا حدود زیادی مشابه با نتایج پیشنهادشده توسط نرم‌افزار (75/33 و 84/71 درصد) بود. طبق نتایج به‌دست‌آمده پروتئین هیدرولیزشدۀ دانۀ کدو از قابلیت ضداکسایشی و مهارکنندگی اکسید نیتریک مناسبی برخوردار می‌‌باشد.


AACC. (1999). Approved method of the American association of cereal chemists. St. Paul: America Association of Cereal Chemists.

Bougatef, A., Hajji, M., Balti, R., Lassoued, I., Triki-Ellouz, Y., & Nasri, M. (2009). Antioxidant and free radical-scavenging activities of smooth hound (mustelus mustelus) muscle protein hydrolysates obtained by gastrointestinal proteases. Food Chemistry, 114(4), 1198-1205. doi:

Chen, H.M., Muramoto, K., & Yamauchi, F. (1995). Structural analysis of antioxidative peptides from soybean b-Conglycinin. Journal of Agricultural and Food Chemistry, 43(3), 574-578. doi:

Cho, S.-J., Juillerat, M.A., & Lee, C.H. (2008). Identification of LDL-receptor transcription stimulating peptides from soybean hydrolysate in human hepatocytes. Journal of Agricultural and Food Chemistry, 56(12), 4372-4376. doi:

Coss, A., Cantor, K.P., Reif, J.S., Lynch, C.F., & Ward, M.H. (2004). Pancreatic cancer and drinking water and dietary sources of nitrate and nitrite. American Journal of Epidemiology, 159(7), 693-701. doi:

Davalos, A., Miguel, M., Bartolome, B., & Lopez-Fandino, R. (2004). Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis. Journal of Food Protection, 67(9), 1939-1944. doi:

Etemadi, M., Sadeghi Mahoonak, A.R., Ghorbani, M., & Maghsodlou, Y. (2014). Optimization of hydrolysis conditions of soybean protein isolate to achieve maximum antioxidant activity using response surface method, (Unpublished master's thesis). Gorgan University of Agricultural Sciences and Natural Resources. (in Persian)

Glew, R.H., Glew, R.S., Chuang, L.-T., Huang, Y.-S., Millson, M., Constans, D., & Vanderjagt, D.J. (2006). Amino acid, mineral and fatty acid content of pumpkin seeds (cucurbita spp) and cyperus esculentus nuts in the republic of niger. Plant Foods for Human Nutrition, 61(2), 49-54. doi:

Guerard, F., Guimas, L., & Binet, A. (2002). Production of tuna waste hydrolysates by a commercial neutral protease preparation. Journal of Molecular Catalysis B: Enzymatic, 19-20, 489-498. doi:

Hauser, E., Yam, I., & Yerman, P. (1980). Nitrosamine in leben esmitteln. Swiss Food, 2, 13-22.

Hernandez-Ledesma, B., Davalos, A., Bartolome, B., & Amigo, L. (2005). Preparation of antioxidant enzymatic hydrolysates from a-lactalbumin and b- actoglobulin. Identification of active peptides by HPLC–MS/MS. Journal of Agricultural and Food Chemistry, 53(3), 588-593. doi:

Kaur, M., & Singh, N. (2007). Characterization of protein isolates from different Indian chickpea (cicer arietinum L.) cultivars. Food Chemistry, 102(1), 366-374. doi:

Khantaphant, S., & Benjakul, S. (2008). Comparative study on the proteases from fish pyloric caeca and the use for production of gelatin hydrolysate with antioxidative activity. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 151(4, 410-419. doi:

Khantaphant, S., Benjakul, S., & Ghomi, M.R. (2011a). The effects of pretreatments on antioxidative activities of protein hydrolysate from the muscle of brownstripe red snapper (lutjanus vitta). LWT-Food Science and Technology, 44(4), 1139-1148. doi:

Khantaphant, S., Benjakul, S., & Kishimura, H. (2011b). Antioxidative and ACE inhibitory activities of proteinhydrolysates from the muscle of brownstripe red snapper prepared sing pyloric caeca and commercial proteases. Process Biochemistry, 46(1), 318-327. doi:

Kim, E.K, Kim, Y.S, Hwang, J.W, Kang, S.H, Choi, D.K, Lee, K.H, Lee, J.S, Moon, S.H, Jeon, B.T, & Park, P.J. (2013). Purification of a novel nitric oxide inhibitory peptide derived from enzymatic hydrolysates of mytilus coruscus. Fish & Shellfish Immunology, 34(6), 1416-1420. doi:

Klompong, V., Benjakul, S., Yachai, M., Visessanguan, W., Shahidi, F., & Hayes, K.D. (2009). Amino acid composition and antioxidative peptides from protein hydrolysates of yellow stripe trevally (selaroides leptolepis). Journal of Food Science, 74(2), 126-133. doi:

Korhnen, H., & Pihlanto, A. (2006). Bioactive peptides: production and functionality. International Dairy Journal, 16(9), 945-960. doi:

Kou, X., Gao, J., Xue, Z., Zhang, Z., Wang, H., & Wang, X. (2013). Purification and identification of antioxidant peptides from chickpea (cicer arietinum L.) albumin hydrolysates. LWT-Food Science and Technology, 50(2), 591-598. doi:

Lee, S.J., Kim, E.K., Kim, Y.S., Hwang, J.W., Lee, K.H., Choi, D.K., Kang, H., Moon, S.H., Jeon, B.T., & Park, P.J. (2012). Purification and characterization of a nitric oxide inhibitory peptide from ruditapes philippinarum. Food and Chemical Toxicology, 50(5), 1660-1666. doi:

Li, G.H., Qu, M.R., Wan, J.Z., & You, J.M. (2007). Antihypertensive effect of rice protein hydrolysate with in vitro angiotensin I-converting enzyme inhibitory activity in spontaneously hypertensive rats. Asia Pacific Journal of Clinical Nutrition, 16(S1), 275-280.

del Castillo, M.D., Ferrigno, A., Acampa, I., Borrelli, R.C., Olano, A., Martinez-Rodriguez, A., & Fogliano, V. (2007). In vitro release of angiotensin-converting enzyme inhibitors, peroxyl-radical scavengers and antibacterial compounds by enzymatic hydrolysis of glycated gluten. Journal of Cereal Science, 45(3), 327-334. doi:

Mazloomi, S.N., & Sadeghi Mahoonak, A.R. (2017). Characterization of nutritional properties of protein isolate of pumpkin (cucurbita pepo con. pepo var styriaca) seeds. Iranian Journal of Food Science and Technology, 70(14), 13-25. (in Persian)

Mehregan Nikoo, A.R., Sadeghi Mahoonak, A.R., Ghorbani, M., Taheri, A., & Alami, M. (2013). Optimization of different factors affecting antioxidant activity of crucian carp (carassius carassius) protein hydrolysate by response surface methodology. Electronic Journal of Food Processing and Peservation, 5(1), 95-110. (in Persian)

Meisel, H., & FitzGerald, RJ. (2003). Biofunctional peptides from milk proteins, mineral binding and cytomodulatory effects. Current Pharmaceutical Design, 9(16), 1289-1296. doi:

Mohamed, R.A., Ramadan, R.S., & Ahmed, L.A. (2009). Effect of substituting pumpkin seed protein isolate for casein on serum liver enzymes, lipid profile and antioxidant enzymes in CCl4-intoxicated rats. Advances in Biological Research, 3(1-2), 9-15.

Nourmohammadi, E., Sadeghi Mahoonak, A.R., Sadeghi, M., Aalami, M., & Ghorbani, M. (2016). Identification of the optimum conditions to anti-oxidative peptides production through the enzymatic hydrolysis of pumpkin oil cake protein by pepsin. Iranian Journal of Food Science and Technology, 61(13), 123-130. (in Persian)

Ohinata, K., Agui, S., & Yoshikawa, M. (2007). Soymorphins, novel m opioid peptides derived from soy β-conglycinin β-subunit, have anxiolytic activities. BioScientific, Biotechnology and Biochemistry, 71(10):2618-2621. doi:

Ovissipour, M., Abedian, A., Motamedzadegan, A., Rasco, B., Safari, R., & Shahiri, H. (2009). The effect of enzymatic hydrolysis time and temperature on the properties of protein hydrolysates from Persian sturgeon (acipenser persicus) viscera. Food Chemistry, 115(1), 238-242. doi:

Parvaneh, V. (2006). Quality control and chemical analysis of food. (pp.332):Tehran University Publication, (in Persian)

Phelan, M., Khaldi, N., Shields, D.C., & Kerins, D.m. (2014). Angiotensin converting enzyme and nitric oxide inhibitory activities of novel milk derived peptides. International Dairy Journal, 35(1), 38-42. Doi:

Phelan, M., Aherne, A., FitzGerald, R.J, & O'Brien, N.M. (2009). Casein-derived bioactive peptides:biological effects, uses, safety aspects and regulatory status. International Dairy Journal, 19(11): 643-654. doi:

Piri Ghashlaghi, Sh., Sadeghi Mahoonak, A.R., Ghorbani, M, & Aalami, M. (2015). Production of bioactive peptides with high antioxidant activity from whey protein concentrate. Journal of Research and Innovation in Food Science and Technology, 3(4), 271-282. doi: (in Persian)

Sun, Q., Shen, H., & Luo, Y. (2011). Antioxidant activity of hydrolysates and peptide fractions derived from porcine hemoglobin. Journal of Food Science and Technology, 48(1):53-60. doi:

Taheri, A., Abedian Kenari, A., Motamedzadegan, A., & Habibi-Rezaei, M. (2011). Poultry by-products and enzymatic hydrolysis: optimization by response surface methodology using alcalase® 2.4L. International Journal of Food Engineering, 7(5), 1-17. doi:

Tsai, P.J., Tsai, T.H., Yu, C.H., & Ho, S.C. (2007). Comparison of no-scavenging and no-suppressing activity of different herbal teas with those of green tea. Food Chemistry, 103(1), 181-187. doi:

Villanueva, A., Vioque, J., Sanchez-Vioque, R., Clemente, A., Pedroche, J., Bautista, J., & Millan, F. (1999). Peptide characteristics of sunflower protein hydrolysates. Journal of the American Oil Chemists’ Society, 76(12), 1455-1460. doi:

Zivanovic, I., Vastag, Z., Popovic, S., Popovic, L., & Pericin, D. (2011). Hydrolysis of hull-less pumpkin oil cake protein isolate by pepsin. International Journal of Biological, Biomolecular, Agricultural, Food and Biotechnological Engineering, 5(3), 94-98. doi: