With increased demand for plant based proteins by the consumers , the food manufacturers appeal for the new plant proteins with predetermined characteristics. This study aims at isolating the protein fraction from jackfruit seeds and characterizing the protein powder for functional and physicochemical properties. The protein part of the seeds was separated through pH treatments and centrifugation process and finally, the concentrate was converted into powder by spray drying method. The functional properties such as solubility, gelling capacity and emulsion properties and the physicochemical properties such as crystallinity, morphology and particle size distribution of the jackfruit seeds protein isolate (JSPI) were studied. The secondary structural elements of JSPI were also determined by Fourier-transform infrared (FTIR) spectroscopy. About 76.89% protein was estimated in the prepared JSPI with 78.44% solubility in an aquatic solvent. The least gelation concentration of JSPI was 12% in a salt solution. The pH of the solvent significantly affected the emulsifying and foaming properties. The protein isolate possessed amorphous structure, moderate bulk density and almost 75% of the particles fell in a similar size distribution range. The conformational study reported that the <i> β </i> -sheet is the dominant secondary structural element with the highest content of 50.28%. The observed features suggest that the JSPI holds satisfactory functional and physicochemical characteristics for being used in protein-enriched foods.
Houde, M., Khodaei, N., Benkerroum, N. and Karboune, S. (2018) Barley Protein Concentrates: Extraction, Structural and Functional Properties. Food Chemistry, 254, 367-376. https://doi.org/10.1016/j.foodchem.2018.01.156
Idris, W.H., Babiker, E.E. and Tinay, A.H.E. (2003) Fractionation, Solubility and Functional Properties of Wheat Bran Proteins as Influenced by pH and/or Salt Concentration. Molecular Nutrition, Food Research, 47, 425-429. https://doi.org/10.1002/food.200390094
Kaushik, P., Dowling, K., McKnight, S., Barrow, C., Wang, B. and Adhikari, B. (2016) Preparation, Characterization and Functional Properties of Flaxseed Protein Isolate. Food Chemistry, 197, 212-220. https://doi.org/10.1016/j.foodchem.2015.09.106
Joshi, M., Adhikari, B., Aldred, P., Panozzo, J.F. and Kasapis, S. (2011) Physicochemical and Functional Properties of Lentil Protein Isolates Prepared by Different Drying Methods. Food Chemistry, 129, 1513-1522. https://doi.org/10.1016/j.foodchem.2011.05.131
Miah, M.Y., Bhattacharjee, S., Sultana, A., Bhowmik, S., Sarker, A.K., Paul, S.C., Islam, M.S. and Zaman, A. (2017) Evaluation of Amino Acid Profile of Jackfruit (Artocarpus heterophyllus) Seed and Its Utilization for Development of Protein Enriched Supplementary Food. Journal of Noakhali Science and Technology University, 1, 77-84.
Ocloo, F.C.K., Bansa, D., Boatin, R., Adom, T. and Agbemavor, W.S. (2010) Physico-Chemical, Functional and Pasting Characteristics of Flour Produced from Jackfruits (Artocarpus heterophyllus Lam.) Seeds. Agriculture and Biology Journal of North America, 1, 903-908. https://doi.org/10.5251/abjna.2010.1.5.903.908
BBS (2016) Yearbook of Agricultural Statistics of Bangladesh. Planning Division, Ministry of Planning, Peoples Republic of Bangladesh, Dhaka.
Kinsella, J.E. (1979) Functional Properties of Soy Proteins. Journal of the American Oil Chemists’ Society, 56, 242-249. https://doi.org/10.1007/BF02671468
Mcwatters, K.H. and Cherry, J.P. (1977) Emulsification, Foaming and Protein Solubility Properties of Defatted Soybean, Peanut, Field Pea and Pecan Flours. Journal of Food Science, 42, 1444-1447. https://doi.org/10.1111/j.1365-2621.1977.tb08395.x
Zayas, J.F. and Lin, C.S. (1989) Emulsifying Properties of Corn Germ Proteins. Cereal Chemistry, 66, 263-267.
Haque, M.A., Aldred, P., Chen, J. and Adhikari, B. (2015). Denaturation and Physical Characteristics of Spray Dried Whey Protein Isolate Powders Produced in the Presence and Absence of Lactose, Trehalose and Polysorbate-80. Drying Technology, 33, 1243-1254. https://doi.org/10.1080/07373937.2015.1023311
Ji, Y.-Y. and Li, Y.-Q. (2010) The Role of Secondary Structure in Protein Structure Selection. The European Physical Journal, Soft Matter, 32, 103-107. https://doi.org/10.1140/epje/i2010-10591-5
Haque, M.A., Aldred, P., Chen, J., Barrow, C. and Adhikari, B. (2014) Drying and Denaturation Characteristics of α-Lactalbumin, β-Lactoglobulin and Bovine Serum Albumin in a Convective Drying Process. Journal of Agricultural and Food Chemistry, 62, 4695-4706. https://doi.org/10.1021/jf405603c
Anandharamakrishnan, C., Rielly, C.D. and Stapley, A.G.F. (2007) Effects of Process Variables on the Denaturation of Whey Proteins during Spray Drying. Drying Technology, 25, 799-807. https://doi.org/10.1080/07373930701370175
Farrell Jr., H.M., Wickham, E.D., Unruh, J.J., Qi, P.X. and Hoagland, P.D. (2001) Secondary Structural Studies of Bovine Caseins: Temperature Dependence of β-Casein Structure as Analyzed by Circular Dichroism and FTIR Spectroscopy and Correlation with Micellization. Food Hydrocolloids, 15, 341-354. https://doi.org/10.1016/S0268-005X(01)00080-7
Abdul-Fattah, A.M., Kalonia, D.S. and Pikal, M.J. (2007) The Challenge of Drying Method Selection for Protein Pharmaceuticals: Product Quality Implications. Journal of Pharmaceutical Sciences, 96, 1886-1915. https://doi.org/10.1002/jps.20842
Chavez, B.E. and Ledeboer, A.M. (2007) Drying of Probiotics: Optimization of Formulation and Process to Enhance Storage Survival. Drying Technology, 25, 1193-1201. https://doi.org/10.1080/07373930701438576
Resendiz-Vazquez, J.A., Ulloa, J.A., Urías-Silvas, J.E., Bautista-Rosales, P.U., Ramírez-Ramírez, J.C., Rosas-Ulloa, P. and González-Torres, L. (2017) Effect of High-Intensity Ultrasound on the Technofunctional Properties and Structure of Jackfruit (Artocarpus heterophyllus) Seed Protein Isolate. Ultrasonics Sonochemistry, 37, 436-444. https://doi.org/10.1016/j.ultsonch.2017.01.042
Resendiz-Vazquez, J.A., Urías-Silvas, J.E., Ulloa, J.A., Bautista-Rosales, P.U. and Ramírez-Ramírez, J.C. (2019) Effect of Ultrasound-Assisted Enzymolysis on Jackfruit (Artocarpus heterophyllus) Seed Proteins: Structural Characteristics, Technofunctional Properties and the Correlation to Enzymolysis. Journal of Food Processing & Technology, 10, 796.
Chowdhury, A.R., Bhattacharyya, A.K. and Chattopadhyay, P. (2014) Functional and Nutritional Characterization of Jackfruit Seed Flour under Different Drying Conditions. Proceedings of the International Conference of Food Properties, Kuala Lumpur, Malaysia, January 2014, 24-26.
Ulloa, J.A., Barbosa, M.C.V., Resendiz-Vazquez, J.A., Rosas-Ulloa, P., Ramírez-Ramírez, J.C., Carrillo, Y.S. and Torres, L.G. (2017) Production, Physico-Chemical and Functional Characterization of a Protein Isolate from Jackfruit (Artocarpus heterophyllus) Seeds. Cyta-Journal of Food, 15, 497-507. https://doi.org/10.1080/19476337.2017.1301554
AOAC (1984) Official Methods of Analysis. 14th Edition, Association of Official Agricultural Chemists, Washington DC.
Beuchat, L.R., Cherry, J.P. and Quinn, M.R. (1975) Physicochemical Properties of Peanut Flour as Affected by Proteolysis. Journal of Agricultural and Food Chemistry, 23, 616-620. https://doi.org/10.1021/jf60200a045
Carcea, B.M. (1986) Functional Properties of Drum Dried Chickpea (Cicer arictinum L). Journal of Food Science, 51, 1518-1526. https://doi.org/10.1111/j.1365-2621.1986.tb13849.x
Coffman, C. and Gracia, V.V. (1977) Functional Properties and Amino Acid Content of Protein Isolate from Mug Bean Flour. Journal of Food Science and Technology, 12, 473-478. https://doi.org/10.1111/j.1365-2621.1977.tb00132.x
Aruna, V. and Prakash, V. (1993) Functional Properties of the Total Proteins of Sunflower (Helianthus annuus L.) Seeds-Effect of Physical and Chemical Treatments. Journal of Agricultural and Food Chemistry, 41, 18-23. https://doi.org/10.1021/jf00025a005
Pearce, K.N. and Kinsella, J.E. (1978) Emulsifying Properties Of Proteins: Evaluation of a Turbidimetric Technique. Journal of Agricultural and Food Chemistry, 26, 716-723. https://doi.org/10.1021/jf60217a041
Gunasekaran, S., Ko, S. and Xiao, L. (2007) Use of Whey Proteins for Encapsulation and Controlled Delivery Applications. Journal of Food Engineering, 83, 31-40. https://doi.org/10.1016/j.jfoodeng.2006.11.001
Jayasundera, M., Adhikari, B., Howes, T. and Aldred, P. (2011) Surface Protein Coverage and Its Implications on Spray-Drying of Model Sugar-Rich Foods: Solubility, Powder Production and Characterisation. Food Chemistry, 128, 1003-1016. https://doi.org/10.1016/j.foodchem.2011.04.006
Boye, J.I. and Alli, I. (2000) Thermal Denaturation of Mixtures of α-Lactalbumin and β-Lactoglobulin: A Differential Scanning Calorimetric Study. Food Research International, 33, 673-682. https://doi.org/10.1016/S0963-9969(00)00112-5
Archer, D.G. (2003) Enthalpy of Fusion of Indium: A Certified Reference Material for Differential Scanning Calorimetry. Journal of Chemical & Engineering Data, 48, 1157-1163. https://doi.org/10.1021/je030112g
Ngarize, S., Herman, H., Adams, A. and Howell, N. (2004) Comparison of Changes in the Secondary Structure of Unheated, Heated, and High-Pressure-Treated β-Lactoglobulin and Ovalbumin Proteins Using Fourier Transform Raman Spectroscopy and Self-Deconvolution. Journal of Agricultural and Food Chemistry, 52, 6470-6477. https://doi.org/10.1021/jf030649y
Haque, M.A., Aldred, P., Chen, J. and Adhikari, B. (2015) Drying and Denaturation Characteristics of Whey Protein Isolate in the Presence of Lactose and Trehalose. Food Chemistry, 177, 8-16. https://doi.org/10.1016/j.foodchem.2014.12.064
Kong, J. and Yu, S. (2007) Fourier Transforms Infrared Spectroscopic Analysis of Protein Secondary Structures. Acta Biochimica et Biophysica Sinica, 39, 549-559. https://doi.org/10.1111/j.1745-7270.2007.00320.x
Sogi, D.S., Garg, S.K. and Bawa, A.S. (2002) Functional Properties of Seeds Meals and Protein Concentrates from Tomato Processing Waste. Journal of Food Science, 67, 2997-3001. https://doi.org/10.1111/j.1365-2621.2002.tb08850.x
Chandi, G.K. and Sogi, D.S. (2007) Functional Properties of Rice Bran Protein Concentrate. Journal of Food Engineering, 79, 592-597. https://doi.org/10.1016/j.jfoodeng.2006.02.018
Naumann, D. (2000) FT-Infrared and FT-Raman Spectroscopy in Biomedical Research. In: Gremlich, H.U. and Yan, B., Eds., Infrared and Raman Spectroscopy of Biological Materials, Marcel Dekker, Inc., Basel, 323-377.
Grube, M., Bekers, M., Upite, D. and Kaminska, E. (2002) Infrared Spectra of Some Fructans. Spectroscopy, 16, 289-296. https://doi.org/10.1155/2002/637587
Susi, H. and Byler, D.M. (1986) Resolution-Enhanced Fourier Transform Infrared Spectroscopy of Enzymes. Methods in Enzymology, 130, 290-311. https://doi.org/10.1016/0076-6879(86)30015-6
Surewicz, W.K. and Mantsch, H.H. (1988) New Insight into Protein Secondary Structure from Resolution-Enhanced Infrared Spectra. Biochimica et Biophysica Acta, 952, 115-130. https://doi.org/10.1016/0167-4838(88)90107-0
Chiou, D., Langrish, T. A. G. and Braham, R. (2008) Partial Crystallization Behavior during Spray Drying: Simulations and Experiments. Drying Technology, 26, 27-38. https://doi.org/10.1080/07373930701781181
Ragab, D.M., Babiker, E.E. and Eltinay, A.H. ( 2004) Fractionation, Solubility and Functional Properties of Cowpea (Vigna unguiculata) Proteins as Affected by pH and/or Salt Concentration. Food Chemistry, 84, 207-212. https://doi.org/10.1016/S0308-8146(03)00203-6
Onimawo, I.A. and Egbekun, N.M. (1998) Comprehensive Food Science and Nutrition. Ambik Publishers, Benin City, 103-220.
Kaur, M. and Singh, N. (2007) Characterization of Protein Isolates from Different Indian Chickpea (Cicer arietinum L.) Cultivars. Food Chemistry, 102, 366-374. https://doi.org/10.1016/j.foodchem.2006.05.029
N-Nadozie, E.F., Kelechi, A.J. and Deborah, O. (2015) Effects pH and NaCl on the Protein Solubility, Emulsifying and Foaming Properties of Germinated and Ungerminated Melon (Colocynthis citrullus) Seeds Flour. International Journal of Food Science and Nutrition, 4, 173-177. https://doi.org/10.11648/j.ijnfs.20150402.18
Damodaran, S. (1990) Interfaces, Protein Films and Foams. Advances in Food Nutrition Research, 34, 1-79. https://doi.org/10.1016/S1043-4526(08)60006-6
Meuser, F., Busch K, G., Fuhrmeister, H. and Rubach, K. (2001) Foam Forming Capacity of Substances Present in Rye. Cereal Chemistry, 78, 50-54. https://doi.org/10.1094/CCHEM.2001.78.1.50
Hung, S.C. and Zayas, J.F. (1991) Emulsifying Capacity and Emulsion Stability of Milk Proteins and Corn Germ Protein Flour. Journal of Food Science, 56, 1216-1223. https://doi.org/10.1111/j.1365-2621.1991.tb04737.x
Dissanayake, M., Liyanaarachchi, S. and Vasiljevic, T. (2012) Functional Properties of Whey Proteins Microparticulated at Low pH. Journal of Dairy Science, 95, 1667-1679. https://doi.org/10.3168/jds.2011-4823
Wang, Q., Du, Y., Hu, X., Yang, J., Fan, L. and Feng, T. (2006) Preparation of Alginate/Soy Protein Isolate Blend Fibers through a Novel Coagulating Bath. Journal of Applied Polymer Science, 101, 425-431. https://doi.org/10.1002/app.22369
Sharma, V.K. and Kalonia, D.S. (2004) Effect of Vacuum Drying on Protein-Mannitol Interactions: The Physical State of Mannitol and Protein Structure in the Dried State. American Association of Pharmaceutical Scientists, and Technology, 5, 1-12. https://doi.org/10.1007/BF02830578
Hassan, H.M. and Mumford, C.J. (1993) Mechanisms of Drying of Skin-Forming Materials. I. Droplets of Materials Which Gelatinised at High Temperature. Drying Technology, 11, 1713-1750. https://doi.org/10.1080/07373939308916925
Fu, F., Deoliveira, D.B., Trumble, W.R., Sarkar, H.K. and Singh, B.R. (1994) Secondary Structure Estimation of Proteins Using the Amide III Region of Fourier Transform Infrared Spectroscopy: Application to Analyze Calcium Binding-Induced Structural Changes in Calsequestrin. Applied Spectroscopy, 48, 1432-1441. https://doi.org/10.1366/0003702944028065
van de Weert, M., Haris, P.I., Hennink, W.E. and Crommelin, D.J.A. (2001) Fourier Transform Infrared Spectrometric Analysis of Protein Conformation: Effect of Sampling Method and Stress Factors. Analytical Biochemistry, 297, 160-169. https://doi.org/10.1006/abio.2001.5337