ارزیابی ویژگی‌های ساختاری و عملکردی پروتئین سه ژنوتیپ مختلف لوبیا (Phaseolus vulgaris)

نوع مقاله : مقاله پژوهشی

نویسندگان

• نازنین فاطمه رحمتی ¹
• آرش کوچکی ¹
• مهدی وریدی ¹
• رسول کدخدایی ²

¹ گروه علوم و صنایع غذایی، دانشکده کشاورزی، دانشگاه فردوسی مشهد.

² گروه نانو فناوری مواد غذایی، پژوهشکده علوم و صنایع غذایی مشهد.

https://doi.org/10.22067/ifstrj.v1396i1.58213

چکیده

امروزه تقاضا برای استفاده از پروتئین های گیاهی در حال افزیش است زیرا این پروتئین ها منابعی قابل دسترس و ارزان هستند. لذا در این تحقیق پروتئین سه ژنوتیپ مختلف لوبیا (Phaseolu svulgaris) شامل پاچ باقلا (Speckled Sugar)، قرمز (Red Mexican) و سفید (Great Northern) با استفاده از روش قلیایی- اسیدی استخراج و ویژگی‌های ساختاری (الکتروفورز، حلالیت، آب‌گریزی) و عملکردی آنها در سیستم‌های مختلف غذایی (امولسیون، ژل و کف) در دامنه پی اچ 3 تا 7 مورد بررسی قرار گرفت. الکتروفورز پروتئین‌ها نشان داد که فازئولین بخش عمده تشکیل‌دهنده هر سه نوع پروتئین مورد بررسی است. ارزیابی حلالیت پروتئین‌ها نیز مشخص نمود که هر سه پروتئین دارای حلالیت بسیار مناسب هستند بطوری‌که حلالیت پروتئین لوبیا پاچ باقلا در پی‌اچ 7، 83 درصد بود. همچنین بررسی آب‌گریزی سطحی نشان داد که پروتئین لوبیای پاچ باقلا کمترین و پروتئین لوبیا سفید بیشترین آب‌گریزی را دارا بودند (05/0P<). به‌علاوه هر سه پروتئین کمترین آب‌گریزی سطحی را در پی‌اچ 7 نشان دادند. ارزیابی ویژگی‌های عملکردی پروتئین‌ها نیز بیان‌کننده این مطلب بود که توانایی امولسیون‌کنندگی بیشتر تحت تاثیر حلالیت پروتئین و در مقابل توانایی تشکیل ژل و کف‌کنندگی تحت تاثیر آب‌گریزی پروتئین‌ها بوده است بطوری‌که بیشترین ظرفیت امولسیون‌کنندگی برای هر سه پروتئین در پی‌اچ 7 (70-77 درصد) اما بیشترین توانایی تشکیل ژل (6 درصد پروتئین) و کف (130-150 درصد) در پی‌اچ 3 مشاهده گردید. نتایج این پژوهش نشان داد با توجه به تاثیر مستقیم ویژگی‌های ساختاری پروتئین بر عملکرد آن، این ویژگی‌ها باید قبل از انتخاب پروتئین برای استفاده در سیستم‌های مختلف غذایی مورد توجه قرار گیرند.

کلیدواژه‌ها

• پروتئین
• ساختار
• عملکرد
• امولسیون
• ژل
• کف

عنوان مقاله [English]

Structural and functional properties of three genotypes of common bean proteins (Phaseolus vulgaris)

نویسندگان [English]

• Fatemeh Rahmati ¹
• Arash Koocheki ¹
• Mehdi Varidi ¹
• Rassoul Kadkhodaee ²

¹ Department of Food Science and Technology, Ferdowsi University of Mashhad, Iran.

² Department of Food Nanotechnology, Research institute for food science and technology, Iran.

چکیده [English]

Introduction: Proteins are food ingredients with critical functional properties and participation in developing food products. So far, functional properties of several plant proteins such as pea, chickpea and lentil, groundnut, beach pea and bayberry have been investigated. Nowadays, there is an increasing demand for plant proteins because they are available and inexpensive. Legume proteins are important plant protein sources. However, except for soy, due to the inadequate information about their structural and functional properties, they do not have appropriate application as functional ingredients in food products. Beans are a great source of nutrients such as protein, carbohydrate, dietary fiber, minerals and vitamins. Based on the several research reports, different dry beans have 15-25% protein and they are the second group of legume seeds, after soy, cultivated throughout the world. As mentioned earlier, insufficient information about structure of legume proteins is the main reason why they are unexploited in food industry. Therefore, the goal of this research was to evaluate the functional properties of proteins from three types of common bean (Speckled Sugar, Red Mexican and Great Northern bean). We also have attempted to evaluate the structure-function relation of these three sources of bean proteins because it is known that there is a direct relation between chemical conformation and the function of a protein which must be considered in food processing. Materials and methods: Protein of three types of common bean (Speckled Sugar, Red Mexican, and Great Northern) was extracted (pH 9, water flour 10:1). Afterwards, their physicochemical (including protein electrophoresis pattern, solubility, hydrophobicity), and functional properties (including emulsifying capacity, heat stability, gelation and foaming capacity) were evaluated to understand how bean protein structure influences its structure. Electrophoresis pattern was obtained based on 2 dimensions (pH and molecular weight). Protein solubility was evaluated by biuret method at pH range 3-9. ANS (8-anilino-1-naphthalenesulfonic acid) was used to measure surface hydrophobicity (pH 3-7).Emulsion samples (1% protein, 25% sunflower oil, pH 3-7) were produced, then emulsion capacity and emulsion heat stability (80°C for 30 min) were evaluated. Gelation of proteins was evaluated at protein concentration of 4-12% at different pH values (3-7). Foaming capacity (%) was measured as the difference between volume after and before whipping. Foam stability (%) was recorded during 90 minutes. Results and Discussion: Results showed that all proteins were rich in Phaseolin. In fact, this fraction was the major building fraction of all three bean proteins. Evaluation of solubility indicated that isoelectric point of three proteins was located at acidic pH range (pH 4.5). Results confirmed an indirect relation between protein solubility and hydrophobicity. All three protein isolates, similar to the other legumes protein, were more soluble at alkaline pH, while the highest surface hydrophobicity was observed at pH 3. Generally, Speckled Sugar bean protein had the most solubility, while Great Northern bean protein showed the highest surface hydrophobicity. Among three bean protein isolates, Speckled Sugar bean protein performed better as an emulsifier, whereas Great Northern bean protein formed gel at the lowest concentration (6% at pHs 3 and 7). In addition, foaming was higher at acidic pH (pH 3). Therefore, it was concluded that emulsifying capacity is mostly influenced by protein solubility, while gelation and foaming properties are affected by protein hydrophobicity. As the main consequence, the results achieved in this research confirmed that there is a direct relation between structure and the function of a protein. In fact, special structural properties are responsible for special functions.

کلیدواژه‌ها [English]

• Protein
• Structure
• function
• Emulsion
• Gel
• Foam

مراجع

Adebowale, K. O., &Lawal, O. S., 2003, Foaming, gelation and electrophoretic characteristics of macuna bean (Macunapruriens) protein concentrate. Food Chemistry, 83, 237-246.

Aluko, R. E., Mofolasayo, O. A., & Watts, B. M., 2009, Emulsifying and foaming properties of commercial yellow pea (Pisumsativum L.) seed flours. Journal of Agricultural and Food Chemistry, 57 (20), 9793–9800.

Asadpoor, A., Jafari, S. M., Sadeghi Mahoonak, A. Ghorbani, M., 2011, Evaluaion of emulsifying capacity and effect of acidity and ionic strength on different legume flours. Iranian Food Science and Technology Research Journal, 6 (3), 80-91.

Bagheri, A., Mahmoudi, A., & Ghezeli, F., 2001, Common beans, research for crop improvement, Mashhad, JDMPress, pp: 10-38.

Bengoechea, C., Romero, A., Aguilar, J. M., Cordobes, F., & Guerrero, A., 2010. Temperature and pH as factors influencing droplet size distribution and linear visco-elasticity of O/W emulsions stabilized by soy and gluten proteins. Food Hydrocolloids, 24 (), 783–791.

Boye, J. I., Aksay, S., Roufik, S., Ribereau, S., Mondor, M., Farnworth, E., &Rajamohamed, S. H., 2010, Comparison of the functional properties of pea, chickpea and lentil protein concentrates processed using ultrafiltration and isoelectric precipitation techniques. Food Research International, 43 (2), 537–546.

Chang, C., Tu, S., Ghosh, S., & Nickerson, M. T., 2015, Effect ofpH on the inter-relationships between the physicochemical, interfacial and emulsifying properties for pea, soy, lentil and canola protein isolates. Food Research International, 77 (3), 360-367.

Cheng, J., Zhou, S., Wu, D., Chen, J., Liu, D., & Ye, X., 2009, Bayberry (MyricarubraSieb. etZucc.) kernel: A new protein source.Food Chemistry, 112 (2), 469–473.

Cherry, J. P. &McWaters, K. H., 1981,Whippability and aeration, In: Cherry, P. (ed.), Protein Functionality in Foods, ACS Symposium Series 147,Washington, pp: 205-304.

Damodaran, S., 1994, Structure function relationship of food proteins, In: Hettiarachchy, N.S. & Gregory, R. (ed.), Protein functionality in food systems, Florida, CRC Press, pp: 1-33.

Depree, J. A., & Savage, G. P., 2001,physical and flavour stability of mayonnaise. Trends in Food Science & Technology, 12 (5), 157–163.

Dziuba, J., Szerszunowicz, I., Nalecz, D., &Dziuba, M., 2014, Proteomic analysis of albumin and globulin fractions of pea (Pisumsativum L.) seeds.ActaScientiarumPolonorumTechnologiaAlimentaria, 13 (2), 181-190.

Eltayeb, A. R. S. M, Ali, A. O., Abou-Arab, A. A., & Abu-Salem, F. M., 2011,Chemical composition and functional properties of flour and protein isolate extracted from Bambara groundnut (Vigna subterranean). African Journal of Food Science, 5 (2), 82 – 90.

Feyzi, S., Varidi, M., Zare, F. & Varidi, M. J., 2013, Study of chemical compositions, color carameters, and functional properties of fenugreek flour and their comparison with those of soy flour. Journal of Research and Innovation in Food Science and Technology, 2 (2), 121-138.

Fennema, O. R., 1996, Food chemistry, New York, Marcel Dekker, pp: 217-330.

Foegeding, E. A., & Davis, J. P., 2011, Food protein functionality: A comprehensive approach. Food Hydrocolloids, 25 (8), 1853-1864.

Fuente, M., Lopez-Pedrouso, M., Alonso, J., Santalla, M. De Ron, A. M., Álvarez, G., & Zapata, C., 2012, In-Depth Characterization of the phaseolin protein diversity of Common bean (phaseolus vulgaris L.) based on two-dimensional electrophoresis and mass spectrometry. Food Technol. Biotechnol, 50 (3), 315–325

Ghorbanian, F., 2014, Study of the Effect of grass pea (Lathyrus sativus) protein isolate on physicochemical properties of oil in water emulsion stabilized with xanthan gum. MS thesis, Ferdowsi University of Mashhad.

Ghoush, M. A., Samhourim, M., Al-Holy, M., & Herald, T., 2008, Formulation and fuzzy modeling of emulsion stability and viscosity of gum-protein emulsifier in a model mayonnaise system. Journal of Food Engineering, 84 (2), 348-357.

Hemmati, A., 2011, Management of chemical fertilizers consumption in legumes, Esfahan, Nosooh.

Jarpa-Parraa, M., Bamdada, F., Tiana, Z., Zengb, H., Temellia, F., & Chena, L., 2015, Impact of ph on molecular structure and surface properties of lentil legumin-like protein and its application as foam stabilizer. Colloids and Surfaces B: Bio interfaces, 132, 45–53.

Karaca, A. C., Low, N., & Nickerson, M., 2011, Emulsifying properties of chickpea, faba bean, lentil and pea proteins produced by isoelectric precipitation and salt extraction. Food Research International, 44 (9), 2742–2750.

Lam, R. S.H., & Nickerson, M. T., 2013, Food proteins: A review on their emulsifying properties using a structure–function approach.Food Chemistry, 141 (2), 975–984.

Lin, C. S. &Zayas, J. F., 1987, Protein solubility, emulsifying stability and capacity of two defatted com germ proteins. Journal of Food Science, 52 (6), 1615-1619.

Meng, G., & Ma, C. Y., 2002, Characterization of globulin from phaseolusangularis (red bean). International Journal of Food Science and Technology, 37 (6), 687–695.

McClements, D. J., 2005, Food Emulsions: Principles, Practices, and Techniques, New York, CRC press, pp: 129-166.

Montoya, C. A., Lalles, J. P., Beebe, S., &Leterme, P., 2009, phaseolin diversity as a possible strategy to improve the nutritional value of common beans (Phaseolus vulgaris). Food Research International, 43 (2), 443-449.

Moure, A., Domıngueza, H., Zunigab, M. E., Sotob, C., &Chamy, R., 2002,Characterisation of protein concentrates from pressed cakes of Guevinaavellana (Chilean hazelnut). Food Chemistry, 78 (2), 179–186.

Nakai, S., Li-Chan, E., & Hayakawa, S., 1986, Contribution of protein hydrophobicity to its functionality. Die Nahrung, 30 (3-4), 327-336.

Natarajan, S. S., Pastor-Corralesa, M. A., Khan, F. H., & Garrett, W. M., 2013, Proteomic analysis of common bean (Phaseolus vulgaris L.) by two-dimensional gel electrophoresis and mass spectrometry.Journal of Basic & Applied Sciences,9,424-437.

Owusu-Apenten, R. K., 2002, Food protein analysis Quantitative effects on processing, Marcel Dekker,New York, pp: 47-64.

Papalamprou, E. M., Doxastakis, G. I., & Kiosseoglou, V., 2010,Chickpea protein isolates obtained by wet extraction as emulsifying agents. Journal of the Science of Food Agriculture, 90 (2), 304–313.

Pauling, L., 2001, selected scientific papers (volume 2), World scientific, USA, and pp: 963-1090.

Rahmati, N. F., Koocheki, A., Varidi, M., & Kadkhodaee, R., 2016, Adsorption of Speckled Sugar bean protein isolate at oil-water interface: effect of ionic strength and pH. International Journal of Biological Macromolecules, http:// dx.doi.org /10.1016/j.ijbiomac.2016.11.008.

Sathe, S. K., 2002, Dry bean protein functionality.Critical Reviews in Biotechnology, 22 (2), 175–223.

Scippa, G. S., Rocco, M., Trupiano, D., Viscosi, V., DiMichele, M., Arena, S., Chiiatante, D. &Scaloni, A. 2010. The proteome of lentil (Lens culinarisMedik.) seeds: discriminating between landraces. Electrophoresis, 31 (3), 497-506.

Siddiq, M. &Uebersax, M. A., 2013, Dry beans and pulses production and consumption- an overview, In: Siddiq, M. &Uebersax, M. A. (ed.),Dry beans and pulses production, processing and nutrition, Wiley and Blackwell,Iowa, pp: 205-234.

Thaiphanit, S.,&Anprung, P., 2015, Physicochemical and emulsion properties of edible protein concentrate from coconut (Cocos nucifera L.) processing by-products and the influence of heat treatment. Food Hydrocolloids, 52, 756-765.

Zayas, J., 1997, Functionality of proteins in food.Springer, New York.