ASİDİK VE BAZİK PH-DEĞİŞTİRME UYGULANMIŞ NOHUT PROTEİNLERİNİN TEKNOFONKSİYONEL ÖZELLİKLERİ

Yıl 2024, Cilt: 49 Sayı: 5, 879 - 890, 10.10.2024

Gülşah Karabulut

https://doi.org/10.15237/gida.GD24038

Öz

Bu çalışma, nohut protein izolatı (CPI) üzerindeki pH değiştirme uygulamasının etkisini incelemiştir. Uygulama yapılmamış CPI ile pH 2'ye (pH2) ve pH 12'ye (pH12) değiştirme uygulanmış örnekler sırasıyla %60.25, %25.01 ve %75.48 çözünürlük göstermiştir. Her iki uygulamada su ve yağ bağlama kapasitelerini önemli ölçüde artırmıştır. pH2 ve pH12'de uygulanmış CPI için emülsiyon aktivitesi ve stabilitesi sırasıyla 125 m2/g ve 110 m2/g iken, uygulama yapılmamış örnek için bu değer 75 m2/g’dır. Özellikle, pH12 değiştirme uygulanmış CPI'nin köpük kapasitesi ve stabilitesi, uygulama yapılmamış proteine kıyasla sırasıyla 3.5 ve 8.8 kat artmıştır. pH12 uygulanan CPI ayrıca, uygulama yapılmamış ve pH2 uygulanan CPI'ye göre sırasıyla %14 ve %18 olan jel oluşum konsantrasyonunda en düşük değer olan %10'u göstermiştir. Mikroyapısal analiz, CPI'nin pH değiştirme ile kısmi olarak denatüre olduğunu ortaya koymuş ve pH12 değiştirme uygulamasının CPI'nin fonksiyonel özelliklerini belirgin şekilde artırdığını vurgulamıştır.

Anahtar Kelimeler

Nohut, pH-değiştirme, modifikasyon, bitkisel protein, fonksiyonel

TECHNO-FUNCTIONAL PROPERTIES OF CHICKPEA PROTEIN ISOLATE-TREATED ACIDIC AND BASIC PH-CYCLING

Öz

This study examined the impact of extreme pH-cycling treatments on chickpea protein isolate (CPI). Untreated CPI, along with samples shifted to pH 2 (pH2) and pH 12 (pH12), displayed solubilities of 60.25%, 25.01%, and 75.48%, respectively. Both treatments significantly improved water and oil absorption capacities. Emulsion activity and stability for CPI at pH2 and pH12 were 125 m2/g and 110 m2/g, respectively, versus 75 m2/g for the untreated sample. Notably, the foaming capacity and stability of pH12-treated CPI increased by 3.5 and 8.8 times, respectively, compared to the untreated protein. pH12-treated CPI also demonstrated the lowest gelling concentration at 10%, compared to 14% and 18% for untreated and pH2-treated CPI, respectively. Microstructural analysis revealed partial disintegration of CPI under pH-cycling, underscoring that alkaline pH12-shifting notably enhances functional properties of CPI.

Anahtar Kelimeler

Chickpea, pH-cycling, modification, plant protein, functionality

Kaynakça

• Arzeni, C., Martínez, K., Zema, P., Arias, A., Pérez, O. E., Pilosof, A. M. R. (2012). Comparative study of high intensity ultrasound effects on food proteins functionality. Journal of Food Engineering, 108(3), 463-472.
• Bessada, S. M., Barreira, J. C., Oliveira, M. B. P. (2019). Pulses and food security: Dietary protein, digestibility, bioactive and functional properties. Trends in Food Science & Technology, 93, 53-68.
• Bolontrade, A. J., Scilingo, A. A., Anon, M.C. (2013). Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1. Colloids and Surfaces B: Biointerfaces, 105, 319–327.
• Boye, J., Zare, F., Pletch, A. (2010). Pulse proteins: Processing, characterization, functional properties and applications in food and feed. Food Research International, 43(2), 414-431.
• Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72(1-2), 248-254.
• Cabra, V., Arreguin, R., Vazquez-Duhalt, R., Farres, A. (2007). Effect of alkaline deamidation on the structure, surface hydrophobicity, and emulsifying properties of the Z19 α-zein. Journal of Agricultural and Food Chemistry, 55(2), 439-445.
• Chang, L., Lan, Y., Bandillo, N., Ohm, J. B., Chen, B., Rao, J. (2022). Plant proteins from green pea and chickpea: Extraction, fractionation, structural characterization and functional properties. Food Hydrocolloids, 123, 107165.
• Choe, U., Chang, L., Ohm, J. B., Chen, B., Rao, J. (2022). Structure modification, functionality and interfacial properties of kidney bean (Phaseolus vulgaris L.) protein concentrate as affected by post-extraction treatments. Food Hydrocolloids, 133, 108000.
• Dijkstra, M. J. J., Fokkink, W. J., Heringa, J., van Dijk, E., Abeln, S. (2018). The characteristics of molten globule states and folding pathways strongly depend on the sequence of a protein. Molecular Physics, 116(21-22), 3173-3180.
• Jiang, J., Xiong, Y. L., Chen, J. (2010). pH shifting alters solubility characteristics and thermal stability of soy protein isolate and its globulin fractions in different pH, salt concentration, and temperature conditions. Journal of Agricultural and Food Chemistry, 58(13), 8035-8042.
• Jiang, J., Wang, Q., Xiong, Y. L. (2018). A pH shift approach to the improvement of interfacial properties of plant seed proteins. Current Opinion in Food Science, 19, 50-56.
• Jiang, S., Ding, J., Andrade, J., Rababah, T. M., Almajwal, A., Abulmeaty, M. M., Feng, H. (2017). Modifying the physicochemical properties of pea protein by pH-shifting and ultrasound combined treatments. Ultrasonics Sonochemistry, 38, 835-842.
• Karabulut, G., Feng, H., Yemiş, O. (2022). Physicochemical and antioxidant properties of industrial hemp seed protein isolate treated by high-intensity ultrasound. Plant Foods for Human Nutrition, 77(4), 577-583.
• Karabulut, G., Yemiş, O. (2022). Modification of hemp seed protein isolate (Cannabis sativa L.) by high-intensity ultrasound treatment. Part 1: Functional properties. Food Chemistry, 375, 131843.
• Lee, H., Yildiz, G., Dos Santos, L. C., Jiang, S., Andrade, J. E., Engeseth, N. J., Feng, H. (2016). Soy protein nano-aggregates with improved functional properties prepared by sequential pH treatment and ultrasonication. Food Hydrocolloids, 55, 200-209.
• Li, J., Wu, M., Wang, Y., Li, K., Du, J., Bai, Y. (2020). Effect of pH-shifting treatment on structural and heat induced gel properties of peanut protein isolate. Food Chemistry, 325, 126921.
• Li, Y., Cheng, Y., Zhang, Z., Wang, Y., Mintah, B. K., Dabbour, M., ... Ma, H. (2020). Modification of rapeseed protein by ultrasound-assisted pH shift treatment: Ultrasonic mode and frequency screening, changes in protein solubility and structural characteristics. Ultrasonics Sonochemistry, 69, 105240.
• Malik, M. A., Saini, C. S. (2018). Rheological and structural properties of protein isolates extracted from dephenolized sunflower meal: Effect of high intensity ultrasound. Food Hydrocolloids, 81, 229-241.
• Malomo, S. A., He, R., Aluko, R. E. (2014). Structural and functional properties of hemp seed protein products. Journal of Food Science, 79(8), C1512-C1521.
• Martínez-Velasco, A., Lobato-Calleros, C., Hernández-Rodríguez, B. E., Román-Guerrero, A., Alvarez-Ramirez, J., Vernon-Carter, E. J. (2018). High intensity ultrasound treatment of faba bean (Vicia faba L.) protein: Effect on surface properties, foaming ability and structural changes. Ultrasonics Sonochemistry, 44, 97-105.
• Pearce, K. N., Kinsella, J. E. (1978). Emulsifying properties of proteins: evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry, 26(3), 716-723.
• Resendiz-Vazquez, J. A., Ulloa, J. A., Urías-Silvas, J. E., Bautista-Rosales, P. U., Ramírez-Ramírez, J. C., Rosas-Ulloa, P., González-Torres, L. J. U. S. (2017). Effect of high-intensity ultrasound on the technofunctional properties and structure of jackfruit (Artocarpus heterophyllus) seed protein isolate. Ultrasonics Sonochemistry, 37, 436-444.
• Tang, X., Shen, Y., Zhang, Y., Schilling, M. W., Li, Y. (2021). Parallel comparison of functional and physicochemical properties of common pulse proteins. LWT, 146, 111594.
• Tontul, İ., Kasimoglu, Z., Asik, S., Atbakan, T., Topuz, A. (2018). Functional properties of chickpea protein isolates dried by refractance window drying. International Journal of Biological Macromolecules, 109, 1253-1259.
• Wang, C. H., Damodaran, S. (1991). Thermal gelation of globular proteins: influence of protein conformation on gel strength. Journal of Agricultural and Food Chemistry, 39(3), 433-438.
• Wang, J., Li, Y., Li, A., Liu, R. H., Gao, X., Li, D., ... Xue, Z. (2021). Nutritional constituent and health benefits of chickpea (Cicer arietinum L.): A review. Food Research International, 150, 110790.
• Wang, J., Zhou, X., Li, J., Pan, D., Du, L. (2024). Enhancing the functionalities of chickpea protein isolate through a combined strategy with pH-shifting and cold plasma treatment. Innovative Food Science & Emerging Technologies, 103607.
• Wang, Q., Jin, Y., Xiong, Y. L. (2018). Heating-aided pH shifting modifies hemp seed protein structure, cross-linking, and emulsifying properties. Journal of Agricultural and Food Chemistry, 66(41), 10827-10834.
• Wang, Y., Wang, S., Li, R., Wang, Y., Xiang, Q., Li, K., Bai, Y. (2022). Effects of combined treatment with ultrasound and pH shifting on foaming properties of chickpea protein isolate. Food Hydrocolloids, 124, 107351.
• Wang, Y., Yang, F., Wu, M., Li, J., Bai, Y., Xu, W., Qiu, S. (2020). Synergistic effect of pH shifting and mild heating in improving heat induced gel properties of peanut protein isolate. LWT, 131, 109812.
• Xiong, T., Xiong, W., Ge, M., Xia, J., Li, B., Chen, Y. (2018). Effect of high intensity ultrasound on structure and foaming properties of pea protein isolate. Food Research International, 109, 260-267.
• Yang, X., Li, Y., Li, S., Oladejo, A. O., Ruan, S., Wang, Y., ... Ma, H. (2017). Effects of ultrasound pretreatment with different frequencies and working modes on the enzymolysis and the structure characterization of rice protein. Ultrasonics Sonochemistry, 38, 19-28.
• Yildiz, G., Andrade, J., Engeseth, N.C., Feng, H. (2017). Functionalizing soy protein nano-aggregates with pH-shifting and mano-thermo-sonication. Journal of Colloid and Interface Science, 505, 836-846.
• Zhang, L., Pan, Z., Shen, K., Cai, X., Zheng, B., Miao, S. (2018). Influence of ultrasound-assisted alkali treatment on the structural properties and functionalities of rice protein. Journal of Cereal Science, 79, 204-209.
• Zhang, Y., Wang, B., Zhang, W., Xu, W., Hu, Z. (2019). Effects and mechanism of dilute acid soaking with ultrasound pretreatment on rice bran protein extraction. Journal of Cereal Science, 87, 318-324.
• Zhao, C., Chu, Z., Miao, Z., Liu, J., Liu, J., Xu, X., ... Yan, J. (2021). Ultrasound heat treatment effects on structure and acid-induced cold set gel properties of soybean protein isolate. Food Bioscience, 39, 100827.