بررسی اثر اسید کافئیک و اسید تانیک بر ویژگی های فیزیکوشیمیایی، مورفولوژیکی و استحکام هیدروژل تهیه شده از ژلاتین ماهی سردآبی

نویسندگان
الناز پارسایی 1
عبدالرضا محمدی نافچی 2
لیلا نوری 3
1 دانشجوی دکتری دانشگاه آزاد اسلامی واحد دامغان
2 دانشیار دانشگاه USM مالزی
3 استادیار دانشگاه آزاد اسلامی واحد دامغان
10.52547/fsct.18.111.267
چکیده
ژلاتین اساساً از دناتوراسیون کلاژن بدست می‌آید. ژلاتین‌های بدست آمده از ماهیان سردآبی، دمای ژل‌سازی-ذوب کمی دارند. تیمارهای شیمیایی و فیزیکی را می‌توان جهت اصلاح شبکه ژلاتین از طریق برقراری اتصالات عرضی بین زنجیره‌های ژلاتین، به منظور بهبود خواص ژل، بکار برد. در این تحقیق، توسط اسید تانیک و اسید کافئیک، هر یک در غلظت های 1، 3 و 5 درصد ،اتصالات عرضی در هیدروژل‌های برپایه ژلاتین ماهی سردآبی برقرار شد و تأثیر غلظت‌عوامل اتصال‌دهنده‌ی عرضی بر خواص فیزیکوشیمیایی هیدروژل‌های ژلاتین مورد بررسی قرار گرفت. استحکام ژل و درجه اتصال عرضی، با افزایش غلظت‌اسید تانیک از 1 تا 3 درصد افزایش یافت، که این افزایش در استحکام ژل از N/mm2 00/325 به 62/343 و درجه اتصال عرضی از 01/82 به 99/84 درصد گزارش شد. ولی در سطح بالاتر اسید تانیک، کاهش در میزان استحکام ژل و درجه اتصال عرضی به ترتیب N/mm2 90/301 و 48/75 درصد مشاهده شد. با این حال، این ویژگی‌های هیدروژل‌ها، با افزایش سطوح اسید کافئیک، به طور پیوسته افزایش پیدا کرد (p<0.05). نسبت متورم شدن نیز در اثر تلفیق سطوح مختلف تانیک اسید و کافئیک اسید، کاهش نشان داد. حداکثر میزان نسبت متورم شدن برای شاهد، 1732.30 درصدو حداقل میزان متورم شدن برای اسید تانیک 3 درصد،594.79 درصد بود. ژلاتین‌های اتصال‌یافته‌ی عرضی توسط اسید تانیک به طور قابل توجهی دمای دناتوراسیون را بهبود بخشیده و پایداری حرارتی آن‌ها بیشتر از ژلاتین-اسید کافئیک بود. به طوری که این دما در هیدروژل تیمار نشده 89 درجه سانتی‌گراد بود و در هیدروژل‌های تیمار شده با اسید کافئیک و اسید تانیک، به ترتیب تا دماهای 94 درجه سانتی‌گراد و 98 درجه سانتی‌گراد افزایش یافت. تصاویر میکروسکوپ الکترونی روبشی نمونه‌های هیدروژل بیانگر اسفنجی بودن ساختار هیدروژل‌های برپایه ژلاتین ماهی سردآبی بود. افزودن عوامل اتصال‌دهنده‌ی عرضی، تنها اندازه حفرات موجود در ژلاتین را کمی کاهش داد و تأثیر قابل توجهی نداشت.
کلیدواژه‌ها
هیدروژل
ژلاتین ماهی سردآبی
درجه اتصال عرضی
اسید تانیک
اسید کافئیک

موضوعات

عنوان مقاله English

The effects of caffeic acid and tannic acid on physicochemical, morphological and hydrogel properties of cold-water fish gelatin

نویسندگان English

Elnaz Parsaie 1
Abdorreza Mohammadi Nafchi 2
Leila Nouri 3
1 Postgraduate student, Food Science & Technology Department, Islamic Azad University, Damghan Branch, Damghan, Iran
2 Associate Professor, Food Technology Division, School of Industrial Technology, Universiti Sains, Penang, Malaysia
3 Assistant Professor, Food Science & Technology Department, Islamic Azad University, Damghan Branch, Damghan, Iran
چکیده English

Gelatin is mainly produced by collagen denaturation. Gelatin obtained from cold-water fish has low sol-gel transition temperatures. Chemical and physical treatments can be used to modify the gelatin network by establishing cross-links between the gelatin chains to improve the properties of the gel. In this study, cross-linking in cold-water fish gelatin-based hydrogels was established by tannic acid (TA) and caffeic acid (CA), each at concentrations of 1, 3 and 5%. The effect of CA and TA concentrations on the physicochemical properties of gelatin hydrogels was investigated. The strength of the gel and the degree of crosslinking increased with increasing the concentration of tannic acid from 1 to 3%, which increased the strength of the gel from 325.00 to 343.62 N/mm2 and the degree of crosslinking from 82.01 to 84.99%. At higher levels of tannic acid, a decrease in gel strength and degree of crosslinking was observed 301.90 N/mm2 and 75.48%, respectively. However, these properties of hydrogels increased steadily with increasing levels of caffeic acid (p <0.05). The swelling rate also decreased due to the combination of different levels of tannic acid and caffeic acid. The maximum swelling rate for the control was 1732.30% and the minimum swelling rate for 3% tannic acid was 594.79%. The crosslinked gelatins by tannic acid significantly improved the denaturation temperature and their thermal stability was higher than that of caffeic acid. This temperature was 89° C in untreated hydrogels and increased to 94 °C and 98 °C in caffeic acid and tannic acid treated hydrogels, respectively. Scanning electron microscopy images of the hydrogel samples showed that the structure of the hydrogels based on cold-water fish gelatin was spongy. The addition of crosslinking agents only slightly reduced the pore size of the gelatin and had no significant effect.

کلیدواژه‌ها English

Hydrogel
cold-water fish gelatin
degree of crosslinking
tannic acid
Caffeic acid
[1] Zeppa, C., Gouanve, F. & Espuche, E. 2009. Effect of a plasticizer on the structure of biodegradable starch/clay nanocomposites: thermal, water-sorption and oxygen-barrier properties. Applied Polymer Science, 112: 2044-2056.
[2] Bourtoom, T. 2009. Edible protein films: properties enhancement. International Food Research Journal, 16: 1-9.
[3] Voon, H.C., Bhat, R., Mat. Easa, A., Liong, M.T. & Karim, A.A. 2012. Effect of addition of halloysite of bovine gelatin films. Food Bioprocess Technology, 5: 1766-1774.
[4] Nawapat Detduangchan, T.W. 2011. Effect of UV-treatment on properties of biodegradable film from rice starch. World Academic Science of Engineering and Technology, 5: 9-25.
[5] Voon, H.C., Bhat, R., Mat. Easa, A., Liong, M.T. & Karim, A.A. 2012. Effect of addition of halloysite of bovine gelatin films. Food Bioprocess Technology, 5: 1766-1774.
[6] Kosaraju, S.L., Puvanenthiran, A. & Lillford, P. 2010. Naturally cross linked gelatin gels with modified material properties. Food Research International, 43: 2385-2389.
[7] Zhang, X., Do, M.D., Casey, P., Sulistio, A., Qiao, G.G., Lundin, L., Lillford, P. & Kosaraju, S. 2010a. Chemical cross-linking gelatin with natural phenolic compounds as studied by high-resolution NMR spectroscopy. Biomacromolecules, 11: 1125-1132.
[8] de Carvalho, R.A. & Grosso, C.R.F. 2006. Properties of chemically modified gelatin films. Brazilian Journal of Chemistry Engineering, 23: 45-53.
[9] See, S.F., Hong, P.K., Ng, K.L., Wan Aida, W.M. & Babji, A.S. 2010. Physicochemical properties of gelatins extracted from skins of different freshwater fish species. International Food Research Journal, 17: 809-816.
[10] Irwandi, J., Faridayanti, S., Mohamed, E.S.M., Hamzah, M.S., Torla, H.H. & Che Man, Y.B. 2009. Extraction and characterization of gelatin from different marine fish species in Malaysia. International
Food Research Journal, 16: 381-389.
[11] Sonthornvit, R. & Krochta, J.M. 2000. Water vapor permeability and solubility of films from hydrolyzed whey protein. Food Engineering and Physics Properties, 65: 700-703.
[12] Gonzalez, A., Strumia, M.C., Ines, C. & Igarzabal, A. 2011. Cross-linked soy protein as material for biodegradable films: synthesis, characterization and biodegradation. Journal of Food Engineering, 106: 331-338.
[13] Yi, J.B., Kim, Y.T., Bae, H.J., Whiteside, W.S. & Park, H.J. 2006. Influence of cross linking on properties of fish gelatin films. Journal of Food Science, 71: 376-383.
[14] Bor-Sen, C., Avena-Bustillos, R. J., Bechtel, P. J., Jafri, H., Narayan, R., Imama, S. H., Glenn, G. M. & Orts, W.J. 2008. Cold water fish gelatin films: Effects of cross-linking on thermal, mechanical, barrier, and biodegradation properties. European Polymer Journal, 44: 3748-3753.
[15] Karim, A.A. & Bhat, R. 2009. Fish gelatin: properties, challenges, and prospects as an alternative to mammalian gelatins. Food Hydrocolloids, 23(3): 563-576.
[16] Lowman, A.M. & Dziubla, T.D. 2004. Structural and Dynamic Response of Neutral and Intelligent Networks in Biomedical Environment. Advanced Chemistry Engineering, 29: 75-130.
[17] Cao, N., Fu, Y. & He, J. 2007. Mechanical properties of gelatin films cross-linked, respectively, by ferulic acid and tannin acid. Food Hydrocolloids, 21: 575-584.
[18] Xing, F., Cheng, G., Yi, K. & Ma, L. 2005. Nanoencapsulation of capsaicin by complex coacervation of gelatin, acacia and tannins. Journal of Applied Polymer Science, 96: 2225-2229.
[19] Robbins, R.J. 2003. Phenolic acids in food: an overview of analytical methodology. Journal of Agriculture and Food Chemistry, 51: 2866-2887.
[20] Charlton, A.J., Baxter, N.J., Khan, M.L., Moir, A.J.G., Haslam, E., Davies, A.P. & Williamson, M.P. 2002. Polyphenol/peptide binding and precipitation. Journal of Agriculture and Food Chemistry, 50, 1593-1601.
[21] Araghi, M., Moslehi, Z., Mohammadi Nafchi, A., Mostahsan, A., Salamat, N. & Daraei Garmakhany, A. 2015. Cold water fish gelatin modification by a natural phenolic cross-linker (ferulic acid and caffeic acid). Food Science and Nutrition, 3(5): 370-375.
[22] Tavasoli kofrani,A. & Goli.s.a.h . 2016. Evaluation of crosslinking properties of gelatin nanofiber with caffeic acid as a phenolic compound. The First International Congress and the 24th National Congress of Food Science and Technology of Iran, 7 pages.
[23] Zhao, Y. & Sun, Z. 2018. Effects of gelatin-polyphenol and gelatin-genipin cross-linking on the structure of gelatin hydrogels. International Journal of Food Properties, 1-12.
[24] Yan, M., Li, B., Zhao, X. & Yi, J. 2011. Physicochemical Properties of Gelatin Gels from Walleye Pollock (Theragra Chalcogramma) Skin Cross-Linked by Gallic Acid and Rutin. Food Hydrocolloids, 25: 907-914.
[25] Charulatha, V. & Rajaram, A. 2003. Influence of Different Crosslinking Treatments on the Physical Properties of Collagen Membranes. Biomaterials, 24: 759-767.
[26] Bubnis, W.A. & Ofner, C. M. 1992. The Determination of ϵ-Amino Groups in Soluble and Poorly Soluble Proteinaceous Materials by a Spectrophotometric Method Using Trinitrobenzenesulfonic Acid. Analysis Biochemistry, 207: 129-133.
[27] Hu, Y., Liu, L., Dan, W., Dan, N., Gu, Z. & Yu, X. 2013. Synergistic Effect of Carbodiimide and Dehydrothermal Crosslinking on Acellular Dermal Matrix. International Journal of Biology Macromolecule, 55: 221-23Lowman, A.M. & Dziubla, T.D. (2004). Structural and Dynamic Response of Neutral and Intelligent Networks in Biomedical Environment. Advanced Chemistry Engineering, 29: 75-130.
[28] de Carvalho, R.A. & Grosso, C.R.F. 2006. Properties of chemically modified gelatin films. Brazilian Journal of Chemistry Engineering, 23: 45-53.
[29] Usha, R. & Ramasami, T. 2004. The Effects of Urea and N-Propanol on Collagen Denaturation: Using DSC, Circular Dicroism and Viscosity. Thermochimistry Acta, 409: 201-206.
[30] He, L., Mu, C., Shi, J., Zhang, Q., Shi, B. & Lin, W. 2011. Modification of Collagen with a Natural Cross-Linker, Procyanidin. International Journal of Biology Macromolecule, 48: 354-359.
[31] Zhao, Y. & Sun, Z. 2018. Effects of gelatin-polyphenol and gelatin-genipin cross-linking on the structure of gelatin hydrogels. International Journal of Food Properties, 1-12.
[32] Balange, A.K. 2009. Enhancement of Gel Strength of Surimi Using Oxidized Phenolic Compounds. A Thesis Submitted in Fulfillment of the Requirements for the Degree of Doctor of Philosophy in Food Science and Technology, Prince of Songkla University. 238 pp.
[33] Bigi, A., Cojazzi, G., Panzavolta, S., Roveri, N. & Rubini, K. 2002. Stabilization of gelatin films by cross-linking with genipin. Biomaterials, 23: 4827-4832.
[34] Bubnis, W.A. & Ofner, C. M. 1992. The Determination of ϵ-Amino Groups in Soluble and Poorly Soluble Proteinaceous Materials by a Spectrophotometric Method Using Trinitrobenzenesulfonic Acid. Analysis Biochemistry, 207: 129-133.
[35] Benjakul, S., Oungbho, K., Visessanguan, W., Thiansilakul, Y. & Roytrakul, S. 2009. Characteristics of gelatin from the skins of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus. Food Chemistry, 116(2): 445-451.
مجله علوم و صنایع غذایی ایران
دوره 18، شماره 111 - شماره پیاپی 111
اردیبهشت 1400
صفحه 267-277