ارزیابی رابطه وزن مولکولی پپتیدهای زیست‌فعال حاصل از آبکافت آنزیمی سر و پوسته میگوی وانامی (Litopenaeus vannamei) با خواص ضدباکتریایی، آنتی اکسیدانی و عملکردی آن ها
محورهای موضوعی :
علوم و صنایع غذایی
سهیل ریحانی پول
1
,
سکینه یگانه
2
,
رضا صفری
3
1 - دانش‌آموخته دکتری تخصصی، گروه فرآوری محصولات شیلاتی، دانشکده شیلات و محیط زیست، دانشگاه علوم کشاورزی و منابع طبیعی گرگان، گرگان، ایران
2 - استاد، گروه شیلات، دانشکده علوم دامی و شیلات، دانشگاه علوم کشاورزی و منابع طبیعی ساری، ساری، ایران
3 - دانش‌آموخته دکتری تخصصی، گروه فرآوری محصولات شیلاتی، دانشکده شیلات و محیط زیست، دانشگاه علوم کشاورزی و منابع طبیعی گرگان، گرگان، ایران
تاریخ دریافت : 1400/06/25
تاریخ پذیرش : 1400/09/22
تاریخ انتشار : 1400/04/01
کلید واژه:
فعالیت ضدباکتریایی,
وزن مولکولی,
ضایعات میگو,
پپتیدهای زیست‌فعال,
چکیده مقاله :
هدف از تحقیق حاضر تعیین رابطه وزن مولکولی پپتیدهای زیست فعال تولیدشده از ضایعات میگوی وانامی با فعالیت آنتی باکتریایی، آنتی‌اکسیدانی و خواص عملکردی آن ها بود. به این منظور پس از انجام فرایند آبکافت، با استفاده از اولترافیلتراسیون، پپتیدهایی با وزن مولکولی کمتر از 3، بین 3 تا 10 و بیش از 10 کیلودالتون تفکیک و جهت انجام آزمون های مختلف مورد استفاده قرار گرفتند. مطابق نتایج، پپتیدهایی با وزن مولکولی 3 تا 10 کیلودالتون بالاترین فعالیت مهارکنندگی رشد باکتری های باسیلوس سرئوس، اشریشیا کولای و استافیلوکوکوس اورئوس را بروز دادند (05/0>P). بیشترین میزان حلالیت و ظرفیت نگهداری آب مربوط به پپتیدهایی با وزن مولکولی کمتر از 3 کیلودالتون بود (05/0>P). در بین وزن‌های مولکولی مختلف، حداکثر شاخص فعالیت امولسیفایری و پایداری امولسیونی در پپتیدهایی با وزن مولکولی بین 3 تا 10 کیلودالتون اندازه گیری شد (05/0>P). کاراترین پپتیدها ازنظر شاخص فعالیت کف زایی و پایداری کف و همچنین ظرفیت جذب روغن، پپتیدهایی با وزن مولکولی بیش از 10 کیلودالتون بودند (05/0>P). نتایج ارزیابی فعالیت آنتی اکسیدانی (فعالیت مهار رادیکال های آزاد DPPH و ABTS) پپتیدها نشان داد. پپتیدهایی با وزن مولکولی کمتر از 3 کیلودالتون دارای بیشترین خاصیت آنتی اکسیدانی هستند (05/0>P). از یافته های این پژوهش می توان نتیجه گرفت خواص پپتیدهای زیست فعال شدیداً تحت تأثیر وزن مولکولی تغییر می کند و هر کدام از پپتیدها در یک وزن مولکولی خاص دارای بیشترین خاصیت و کارایی هستند.
چکیده انگلیسی:
The current research aimed to determine the relationship between the molecular weight of bioactive peptides produced from Vanami shrimp wastes with their antibacterial, antioxidant activity, and functional properties. For this purpose, after performing the hydrolysis process, using ultrafiltration, peptides with a molecular weight of less than 3, between 3 and 10, and more than 10 kDa were separated and used for various tests. According to the results, peptides with a molecular weight of 3 to 10 kDa showed the highest growth inhibitory activity of Bacillus cereus, Escherichia coli, and Staphylococcus aureus (p< 0.05). The highest solubility and water holding capacity were related to peptides with molecular weight less than 3 kDa (p<0.05). Among different molecular weights, the maximum emulsifying activity and emulsion stability indices were measured in peptides with a molecular weight between 3 and 10 kDa (p<0.05). The strongest peptides in terms of foaming activity and foam stability index as well as oil absorption capacity were peptides with a molecular weight of more than 10 kDa (p<0.05). The results of the evaluation of the antioxidant activity (Free radical scavenging activity of DPPH and ABTS) of peptides showed peptides with a molecular weight of less than 3 kDa have the highest antioxidant properties (p<0.05). It was concluded that the properties of bioactive peptides change considerably under the influence of molecular weight and each of the peptides in a particular molecular weight has more properties and efficiency.
منابع و مأخذ:
Adler-Nissen, J. (1986). Enzymatic hydrolysis of food proteins. London: Elsevier Applied Science. 57–109.
Alemán, A., Pérez-Santín, E., Bordenave-Juchereau, S., Arnaudin, I., Gómez-Guillén, M.C. and Montero, P. (2011). Squid gelatin hydrolysates with antihypertensive, anticancer and antioxidant activity. Food Research International, 44(4): 1044-1051.
Amissah, J. (2012). Bioactive properties of salmon skin protein hydrolysates. (Doctoral dissertation, McGill University Libraries).
Ahmadi, A., Yeganeh, S. and Smaili, M. (2020). nvestigation of antioxidant properties of hydrolyzed protein derived from Common carp (Cyprinus carpio) viscera. Journal of Fisheries, 73 (4): 593-606. [In Persian]
Chobert, J.M., Bertrand-Harb, C. and Nicolas, M.G. (1988). Solubility and emulsifying properties of caseins and whey proteins modified enzymically by trypsin. Journal of Agricultural and Food Chemistry, 36(5), 883-892.
Elavarasan, K., Naveen Kumar, V. and Shamasundar, B.A. (2014). Antioxidant and functional properties of fish protein hydrolysates from fresh water carp (Catla catla) as influenced by the nature of enzyme. Journal of Food Processing and Preservation, 38(3): 1207-1214.
Giménez, B., Gómez-Estaca, J., Alemán, A., Gómez-Guillén, M.C. and Montero, M.P. (2009). Physico-chemical and film forming properties of giant squid (Dosidicus gigas) gelatin. Food Hydrocolloids, 23(3), 585-592.
Jia, J., Ma, H., Zhao, W., Wang, Z., Tian, W., Luo, L. and He, R. (2010). The use of ultrasound for enzymatic preparation of ACE-inhibitory peptides from wheat germ protein. Food Chemistry, 119(1): 336-342.
Kristinsson, H.G. and Rasco, B.A. (2000). Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases. Journal of Agricultural and Food Chemistry, 48(3): 657-666.
Kusumaningtyas, E., Nurilmala, M., & Sibarani, D. (2019). Antioxidant and antifungal activities of collagen hydrolysates from skin of milkfish (Chanos chanos) hydrolyzed using various bacillus proteases. In IOP Conference Series: Earth and Environmental Science, IOP Publishing, Vol. 278, No. 1, p. 012040.
Mahmoud, M.I. (1994). Physicochemical and functional properties of protein hydrosylates in nutritional products. Food Technology, 48(10): 89-95.
Mutilangi, W.A.M., Panyam, D. and Kilara, A. (1996). Functional properties of hydrolysates from proteolysis of heat‐denatured whey protein isolate. Journal of Food Science, 61(2): 270-275.
Nalinanon, S., Benjakul, S., Kishimura, H. and Shahidi, F. (2011). Functionalities and antioxidant properties of protein hydrolysates from the muscle of ornate threadfin bream treated with pepsin from skipjack tuna. Food Chemistry, 124(4): 1354-1362.
Linder, M., Fanni, J. and Parmentier, M. (1996). Functional properties of veal bone hydrolysates. Journal of Food Science, 61(4), 712-716.
Ovissipour, M., Abedian, A., Motamedzadegan, A., Rasco, B., Safari, R. and 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.
Pearce, K.N. and Kinsella, J.E. (1978). Emulsifying properties of proteins: evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry, 26(3): 716-723.
Pearson, A.M. (1983). Soy proteins. In: B.J.F. Hudson (Ed.), Developments in Food Proteins-2, Essex, England: Applied Science Publishers. pp. 67–108.
Park, P.J., Jung, W.K., Nam, K.S., Shahidi, F. and Kim, S.K. (2001). Purification and characterization of antioxidative peptides from protein hydrolysate of lecithin-free egg yolk. Journal of the American Oil Chemists' Society, 78(6): 651-656.
Ramos-Villarroel, A.Y., Soliva-Fortuny, R. and Martın-Belloso, O. (2010). Natural antimicrobials for food processing. Animal Science Reviews,
Rajendran, S. (2012). Biologically active protein hydrolysates from dog fish (Squalus acanthias) skin. Doctoral Dissertation, McGill University.
Reyhani Poul, S. and Jafarpour, A. (2017). Effects of degree of hydrolysis on functional properties and antioxidants activity of hydrolysate from head and frame of common carp (Cyprinus carpio) fish. Iranian Journal of Food Science and Technology, 68 (14): 113-124. [In Persian]
Reyhani Poul, S., Jafarpour, A. and Safari, R. (2018). Study of oil fatty acid profile, functional properties and antioxidants activity of hydrolyzate produced from rainbow trout (Oncorhynchus mykiss) viscera by application protamex and neutrase enzymes. Iranian Food Science and Technology Research Journal. 14 (1): 162-176. [In Persian]
Shahidi, F., Han, X. Q. and Synowiecki, J. (1995). Production and characteristics of protein hydrolysates from capelin (Mallotus villosus). Food Chemistry, 53(3): 285-293.
Sun, J., He, H. and Xie, B. J. (2004). Novel antioxidant peptides from fermented mushroom Ganoderma lucidum. Journal of Agricultural and Food Chemistry, 52(21): 6646-6652.
Shahidi, F. and Zhong, Y. (2008). Bioactive peptides. Journal of AOAC international, 91(4), 914-931.
Šližytė, R., Mozuraitytė, R., Martínez-Alvarez, O., Falch, E., Fouchereau-Peron, M. and Rustad, T. (2009). Functional, bioactive and antioxidative properties of hydrolysates obtained from cod (Gadus morhua) backbones. Process Biochemistry, 44(6): 668-677.
Sila, A., Nedjar-Arroume, N., Hedhili, K., Chataigné, G., Balti, R., Nasri, M., et al. (2014). Antibacterial peptides from barbel muscle protein hydrolysates: Activity against some pathogenic bacteria. LWT-Food Science and Technology, 55(1): 183-188.
Shabanpour, B., Kordjazi, M., Nazari, Kh. and Smaeili, M. (2017). Effect of enzymatic hydrolysis time, temperature and enzyme to substrate ratio on antioxidant properties of prawn bioactive peptides. Iranian Journal of Food Science and Technology, 62(14): 31-45. [In Persian]
Esmaeili Kharyeki, M., Rezaei, M., Khodabandeh, S. and Motamedzadegan, A. (2018). Antioxidant activity of protein hydrolysate in skipjack tuna head. Journal of Fisheries Science and Technology,7(1): 57-64. [In Persian]
Turgeon, S.L., Gauthier, S.F. and Paquin, P. (1991). Interfacial and emulsifying properties of whey peptide fractions obtained with a two-step ultrafiltration process. Journal of Agricultural and Food chemistry, 39(4): 673-676.
Taheri, A., Anvar, S.A.A., Ahari, H. and Fogliano, V. (2013). Comparison the functional properties of protein Hydrolysates from poultry byproducts and rainbow trout (Onchorhynchus mykiss) viscera. Iranian Journal of Fisheries Sciences, 12(1): 154-169.
Wilde, P.J. and Clark, D.C. (1996). The competitive displacement of β-lactoglobulin by Tween 20 from oil-water and air-water interfaces. Journal of Colloid and Interface Science, 155(1): 48-54.
Wasswa, J., Tang, J., Gu, X.H. and Yuan, X.Q. (2007). Influence of the extent of enzymatic hydrolysis on the functional properties of protein hydrolysate from grass carp (Ctenopharyngodon idella) skin. Food Chemistry, 104(4): 1698-1704.
Wald, M., Schwarz, K., Rehbein, H., Bußmann, B. and Beermann, C. (2016). Detection of antibacterial activity of an enzymatic hydrolysate generated by processing rainbow trout by-products with trout pepsin. Food Chemistry, 205: 221-228.
Yen, G.C. and Wu, J.Y. (1999). Antioxidant and radical scavenging properties of extracts from Ganoderma tsugae. Food Chemistry, 65(3): 375-37.
Yeganeh, S., Esmaeili, M. and Ahmadi, H. (2021). Effect of hydrolysis time on the antioxidant activity of Common carp (Cyprinus carpio) head protein hydrolysate. Iranian Scientific Fisheries Journal, 29 (6): 29-42. [In Persian]
Yaghoubzadeh, Z., Kaboosi, H., Peyravii, F., Safari, R. and Fattahi, E. (2021). Evaluation of antibacterial and antioxidant activities of rainbow trout (Oncorhynchus mykiss) skin protein hydrolysate. Iranian Scientific Fisheries Journal, 28 (2), 117-129. [In Persian]
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Adler-Nissen, J. (1986). Enzymatic hydrolysis of food proteins. London: Elsevier Applied Science. 57–109.
Alemán, A., Pérez-Santín, E., Bordenave-Juchereau, S., Arnaudin, I., Gómez-Guillén, M.C. and Montero, P. (2011). Squid gelatin hydrolysates with antihypertensive, anticancer and antioxidant activity. Food Research International, 44(4): 1044-1051.
Amissah, J. (2012). Bioactive properties of salmon skin protein hydrolysates. (Doctoral dissertation, McGill University Libraries).
Ahmadi, A., Yeganeh, S. and Smaili, M. (2020). nvestigation of antioxidant properties of hydrolyzed protein derived from Common carp (Cyprinus carpio) viscera. Journal of Fisheries, 73 (4): 593-606. [In Persian]
Chobert, J.M., Bertrand-Harb, C. and Nicolas, M.G. (1988). Solubility and emulsifying properties of caseins and whey proteins modified enzymically by trypsin. Journal of Agricultural and Food Chemistry, 36(5), 883-892.
Elavarasan, K., Naveen Kumar, V. and Shamasundar, B.A. (2014). Antioxidant and functional properties of fish protein hydrolysates from fresh water carp (Catla catla) as influenced by the nature of enzyme. Journal of Food Processing and Preservation, 38(3): 1207-1214.
Giménez, B., Gómez-Estaca, J., Alemán, A., Gómez-Guillén, M.C. and Montero, M.P. (2009). Physico-chemical and film forming properties of giant squid (Dosidicus gigas) gelatin. Food Hydrocolloids, 23(3), 585-592.
Jia, J., Ma, H., Zhao, W., Wang, Z., Tian, W., Luo, L. and He, R. (2010). The use of ultrasound for enzymatic preparation of ACE-inhibitory peptides from wheat germ protein. Food Chemistry, 119(1): 336-342.
Kristinsson, H.G. and Rasco, B.A. (2000). Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases. Journal of Agricultural and Food Chemistry, 48(3): 657-666.
Kusumaningtyas, E., Nurilmala, M., & Sibarani, D. (2019). Antioxidant and antifungal activities of collagen hydrolysates from skin of milkfish (Chanos chanos) hydrolyzed using various bacillus proteases. In IOP Conference Series: Earth and Environmental Science, IOP Publishing, Vol. 278, No. 1, p. 012040.
Mahmoud, M.I. (1994). Physicochemical and functional properties of protein hydrosylates in nutritional products. Food Technology, 48(10): 89-95.
Mutilangi, W.A.M., Panyam, D. and Kilara, A. (1996). Functional properties of hydrolysates from proteolysis of heat‐denatured whey protein isolate. Journal of Food Science, 61(2): 270-275.
Nalinanon, S., Benjakul, S., Kishimura, H. and Shahidi, F. (2011). Functionalities and antioxidant properties of protein hydrolysates from the muscle of ornate threadfin bream treated with pepsin from skipjack tuna. Food Chemistry, 124(4): 1354-1362.
Linder, M., Fanni, J. and Parmentier, M. (1996). Functional properties of veal bone hydrolysates. Journal of Food Science, 61(4), 712-716.
Ovissipour, M., Abedian, A., Motamedzadegan, A., Rasco, B., Safari, R. and 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.
Pearce, K.N. and Kinsella, J.E. (1978). Emulsifying properties of proteins: evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry, 26(3): 716-723.
Pearson, A.M. (1983). Soy proteins. In: B.J.F. Hudson (Ed.), Developments in Food Proteins-2, Essex, England: Applied Science Publishers. pp. 67–108.
Park, P.J., Jung, W.K., Nam, K.S., Shahidi, F. and Kim, S.K. (2001). Purification and characterization of antioxidative peptides from protein hydrolysate of lecithin-free egg yolk. Journal of the American Oil Chemists' Society, 78(6): 651-656.
Ramos-Villarroel, A.Y., Soliva-Fortuny, R. and Martın-Belloso, O. (2010). Natural antimicrobials for food processing. Animal Science Reviews,
Rajendran, S. (2012). Biologically active protein hydrolysates from dog fish (Squalus acanthias) skin. Doctoral Dissertation, McGill University.
Reyhani Poul, S. and Jafarpour, A. (2017). Effects of degree of hydrolysis on functional properties and antioxidants activity of hydrolysate from head and frame of common carp (Cyprinus carpio) fish. Iranian Journal of Food Science and Technology, 68 (14): 113-124. [In Persian]
Reyhani Poul, S., Jafarpour, A. and Safari, R. (2018). Study of oil fatty acid profile, functional properties and antioxidants activity of hydrolyzate produced from rainbow trout (Oncorhynchus mykiss) viscera by application protamex and neutrase enzymes. Iranian Food Science and Technology Research Journal. 14 (1): 162-176. [In Persian]
Shahidi, F., Han, X. Q. and Synowiecki, J. (1995). Production and characteristics of protein hydrolysates from capelin (Mallotus villosus). Food Chemistry, 53(3): 285-293.
Sun, J., He, H. and Xie, B. J. (2004). Novel antioxidant peptides from fermented mushroom Ganoderma lucidum. Journal of Agricultural and Food Chemistry, 52(21): 6646-6652.
Shahidi, F. and Zhong, Y. (2008). Bioactive peptides. Journal of AOAC international, 91(4), 914-931.
Šližytė, R., Mozuraitytė, R., Martínez-Alvarez, O., Falch, E., Fouchereau-Peron, M. and Rustad, T. (2009). Functional, bioactive and antioxidative properties of hydrolysates obtained from cod (Gadus morhua) backbones. Process Biochemistry, 44(6): 668-677.
Sila, A., Nedjar-Arroume, N., Hedhili, K., Chataigné, G., Balti, R., Nasri, M., et al. (2014). Antibacterial peptides from barbel muscle protein hydrolysates: Activity against some pathogenic bacteria. LWT-Food Science and Technology, 55(1): 183-188.
Shabanpour, B., Kordjazi, M., Nazari, Kh. and Smaeili, M. (2017). Effect of enzymatic hydrolysis time, temperature and enzyme to substrate ratio on antioxidant properties of prawn bioactive peptides. Iranian Journal of Food Science and Technology, 62(14): 31-45. [In Persian]
Esmaeili Kharyeki, M., Rezaei, M., Khodabandeh, S. and Motamedzadegan, A. (2018). Antioxidant activity of protein hydrolysate in skipjack tuna head. Journal of Fisheries Science and Technology,7(1): 57-64. [In Persian]
Turgeon, S.L., Gauthier, S.F. and Paquin, P. (1991). Interfacial and emulsifying properties of whey peptide fractions obtained with a two-step ultrafiltration process. Journal of Agricultural and Food chemistry, 39(4): 673-676.
Taheri, A., Anvar, S.A.A., Ahari, H. and Fogliano, V. (2013). Comparison the functional properties of protein Hydrolysates from poultry byproducts and rainbow trout (Onchorhynchus mykiss) viscera. Iranian Journal of Fisheries Sciences, 12(1): 154-169.
Wilde, P.J. and Clark, D.C. (1996). The competitive displacement of β-lactoglobulin by Tween 20 from oil-water and air-water interfaces. Journal of Colloid and Interface Science, 155(1): 48-54.
Wasswa, J., Tang, J., Gu, X.H. and Yuan, X.Q. (2007). Influence of the extent of enzymatic hydrolysis on the functional properties of protein hydrolysate from grass carp (Ctenopharyngodon idella) skin. Food Chemistry, 104(4): 1698-1704.
Wald, M., Schwarz, K., Rehbein, H., Bußmann, B. and Beermann, C. (2016). Detection of antibacterial activity of an enzymatic hydrolysate generated by processing rainbow trout by-products with trout pepsin. Food Chemistry, 205: 221-228.
Yen, G.C. and Wu, J.Y. (1999). Antioxidant and radical scavenging properties of extracts from Ganoderma tsugae. Food Chemistry, 65(3): 375-37.
Yeganeh, S., Esmaeili, M. and Ahmadi, H. (2021). Effect of hydrolysis time on the antioxidant activity of Common carp (Cyprinus carpio) head protein hydrolysate. Iranian Scientific Fisheries Journal, 29 (6): 29-42. [In Persian]
Yaghoubzadeh, Z., Kaboosi, H., Peyravii, F., Safari, R. and Fattahi, E. (2021). Evaluation of antibacterial and antioxidant activities of rainbow trout (Oncorhynchus mykiss) skin protein hydrolysate. Iranian Scientific Fisheries Journal, 28 (2), 117-129. [In Persian]
