Modifiye Bitkisel Protein İzolatlarının Üretimi
Özet
Proteinler hem metabolik faaliyetler için hem de gıda üretiminde sahip oldukları fonksiyonel özellikler bakımından oldukça önemlidir. Proteinlerin üç boyutlu yapısı özellikle tersiyer yapı oldukça kırılgan konfigürasyonda olup dış faktörlerden etkilenebilir. Yapıdaki bağların kırılması proteinlerin bazı özelliklerini olumsuz yönde etkilerken gıda teknolojisi açısından avantaj sağlayan özellikler de kazandırabilmektedir. Bu nedenle proteinlerin farklı yöntemlerle denatürasyonu ve modifikasyonu önem taşımaktadır. Proteinlerin fonksiyonel özelliklerini artırmak amacıyla gıdalarda doğrudan protein kaynağı yerine protein konsantratlarının veya izolatlarının kullanımı yaygınlaşmaktadır. Protein konsantratı veya izolatı eldesinde baklagiller, yağlı tohumlar ve tahıllar gibi bitkisel kaynaklar, hayvansal kaynaklara göre temini kolay, ucuz ve yaygın olduğundan daha çok tercih edilmektedir. Ayrıca vegan beslenmenin arttığı günümüzde protein eldesinde protein içeriği yüksek bitkisel kaynakların önemi büyüktür. Bu bölümde protein konsantratları ve izolatlarının üretimi ve modifikasyon yöntemleri üzerinde durulacaktır.
Proteins are highly important because both of their metabolic activities and of their functional properties in food production. The three-dimensional structure of proteins, especially the tertiary structure, is quite fragile and can be affected by external factors. While the breakage of bonds in the structure adversely affects some properties of proteins, it can also bring advantageous characteristics to proteins in terms of food technology. Therefore, the denaturation and modification of proteins through various methods are crucial. The use of protein concentrates or isolates in food is becoming more common instead of directly using protein sources to enhance the functional properties of proteins. Obtaining protein concentrates or isolates from plant sources such as legumes, oilseeds, and grains is more preferred due to their easy, inexpensive, and widespread availability compared to animal sources. Additionally, with the increasing trend of vegan diets today, high-protein plant sources in protein production is significant. This section will focus on the production and modification methods of protein concentrates and isolates.
Referanslar
Akharume, F. U., Aluko, R. E., & Adedeji, A. A. (2021) Modification of plant proteins for improved functionality: A review. Comprehensive Reviews in Food Science and Food Safety, 20, 198-224. Doi: 10.1111/1541-4337.12688
Akyüz, A., & Ersus-Bilek S. (2018) Protein Çöktürme Yöntemlerinin Karşılaştırılması. Çukurova Tarım ve Gıda Bilimleri Dergisi, 33 (2), 83-92.
Alonso-Miravalles, L., Jeske, S., Bez, J., et al. (2019) Membrane filtration and isoelectric precipitation technological approaches for the preparation of novel, functional and sustainable protein isolate from lentils. European Food Research and Technology, 245, 1855–1869. Doi: 10.1007/ s00217-019-03296-y
Belitz, H. D., Grosch, W., & Schieberle, P. (2009) Food Chemistry. Almanya: Springer
Ben-Harb, S., Panouillé, M., Huc-Mathis, D., et al. (2018). The rheological and microstructural properties of pea, milk, mixed pea/milk gels and gelled emulsions designed by thermal, acid, and enzyme treatments. Food Hydrocolloids, 77, 75-84. Doi: 10.1016/j.foodhyd.2017.09.022
Cabra, V., Arreguin, R., Vazquez-Duhalt, R., et al. (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. Doi: 10.1021/jf061002r
Chmielewska, A., Kozłowska, M., Rachwał, D., et al. (2021) Canola/rapeseed protein–nutritional value, functionality and food application: A review. Critical Reviews in Food Science and Nutrition, 61 (22), 3836–3856. Doi: 10.1080/10408398.2020.1809342
Choe, U., Lan, Y., Chen, B., et al. (2022) Structural, and functional properties of phosphorylated pea protein isolate by simplified co-spray drying process. Food Chemistry, 393 (1), 133441. Doi: 10.1016/j.foodchem.2022.133441
Onwulata, C. I., Konstance, R. P., Cooke, P.H., et al. (2003) Functionality of extrusion-texturized whey proteins. Journal of Dairy Science, 86, 3775–3782. Doi: 10.3168/jds.S0022-0302(03)73984-8
Demirci, M. (2006). Gıda Kimyası. Tekirdağ: Kelebek Matbaacılık
Dong, S., Gao, A., Zhao, Y., et al. (2017) Characterization of physicochemical and structural properties of atmospheric cold plasma (acp) modified zein. Food and Bioproducts Processing, 106, 65–74. Doi: 10.1016/j.fbp.2017.05.011
Eckert, E., Han, J., Swallow, K., et al. (2019) Effects of enzymatic hydrolysis and ultrafiltration on physicochemical and functional properties of faba bean protein. Cereal Chemistry, 96 (4), 725–741. Doi: 10.1002/cche.10169
Fernando, S. (2022) Pulse protein ingredient modification. Journal of the Science of Food and Agriculture, 102, 892-897. Doi: 10.1002/jsfa.11548
Flores, I., Cabra, V., Quirasco, M. C., et al. (2010) Emulsifying properties of chemically deamidated corn (zea mays) gluten meal. Food Science and Technology International, 16 (3), 241–250. Doi: 10.1177/1082013210366750
Glusac, J., Isaschar-Ovdat, S., & Fishman, A. (2020) Transglutaminase modifies the physical stability and digestibility of chickpea protein-stabilized oil-in-water emulsions. Food Chemistry, 315, 126301. Doi: 10.1016/j.foodchem.2020.126301
Hu, H., Cheung, I. W., Pan, S., et al. (2015) Effect of high intensity ultrasound on physicochemical and functional properties of aggregated soybean β-conglycinin and glycinin. Food Hydrocolloids, 45, 102-110. Doi: 10.1016/j.foodhyd.2014.11.004
Hu, Y., Du, L., Sun, Y., et al. (2023) Recent developments in phosphorylation modification on food proteins: Structure characterization, site identification and function. Food Hydrocolloids, 137, 108390. Doi: 10.1016/j.foodhyd.2022.108390
Jiang, L., Wang, J., Li, Y., et al. (2014) Effects of ultrasound on the structure and physical properties of black bean protein isolates. Food Research International, 62, 595–601. Doi: 10.1016/j.foodres.2014.04.022,
Kandemir, H., Aydın-Kandemir, F., Güler, B., et al. (2021) Soğuk Plazma Teknolojisi ve Tarımdaki Çeşitli Uygulama Alanları. Bursa Uludağ Üniversitesi Ziraat Fakültesi Dergisi, 35 (1), 217-245.
Khan, N. M., Mu, T. H., Sun, H. N., et al. (2015) Effects of high hydrostatic pressure on secondary structure and emulsifying behavior of sweet potato protein. High Pressure Research, 35 (2), 189-202. Doi: 10.1080/08957959.2015.1005013
Kumar, M., Tomar, M., Punia, S., et al. (2022) Plant-based proteins and their multifaceted industrial applications. LWT, 154, 112620. Doi: 10.1016/j.lwt.2021.112620
Lin, S., Huff, H., & Hsieh, F. (2000) Texture and chemical characteristics of soy protein meat analog extruded at high moisture. Journal of Food Science, 65 (2), 264–269. Doi: 10.1111/j.1365-2621.2000.tb15991.x
Ma, Z., Boye, J. I., Simpson, B. K., et al. (2011) Thermal processing effects on the functional properties and microstructure of lentil, chickpea, and pea flours. Food Research International, 44 (8), 2534–2544. Doi: 10.1016/j.foodres.2010.12.017
Martínez-Velasco, A., Lobato-Calleros, C., Hernández-Rodríguez, B. E., et al. (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. Doi: 10.1016/j.ultsonch.2018.02.007
Meganaharshini, M., Sudhakar, V., Dhivya-Bharathi, N., et al. (2023) Review on recent trends in the application of protein concentrates and isolates – A food industry perspective. Food and Humanity, 1, 308-325. Doi:10.1016/j.foohum.2023.05.022
Mehenktaş, C. Süt İşlemede Ultrason Kullanımı. (2022) Akademik Gıda, 20 (4), 474-481.
Messens, W., Van Camp, J., & Huyghebaert, A. (1997) The use of high pressure to modify the functionality of food proteins. Trends in Food Science & Technology, 8 (4), 107–112. Doi: 10.1016/S0924-2244(97)01015-7
Oliveira, F. C. D., Coimbra, J. S. D. R., Oliveira, E. B. D., et al. (2016) Food protein-polysaccharide conjugates obtained via the Maillard reaction: a review. Critical Reviews in Food Science and Nutrition, 56, 1108–1125. Doi: 10.1080/10408398.2012.755669
Ötleş, S., Özdestan-Ocak, Ö., Nakilcioğlu, E., Kartal, C., & Özyurt, V. H. (2015). Gıda Kimyası. İzmir: Ege Üniversitesi Basımevi
Phongthai, S., D’Amico, S., Schoenlechner, R., et al. (2016) Comparative study of rice bran protein concentrate and egg albumin on gluten-free bread properties. Journal of Cereal Science, 72, 38–45. Doi: 10.1016/j.jcs.2016.09.015
Phongthai, S., Lim, S. T., & Rawdkuen, S. (2016) Optimization of microwave-assisted extraction of rice bran protein and its hydrolysates properties. Journal of Cereal Science, 70, 146-154. Doi: 10.1016/j.jcs.2016.06.001
Rasheed, F., Markgren, J., Hedenqvist, M., et al. (2020) Modeling to understand plant protein structure-function relationships-Implications for seed storage proteins. Molecules, 25 (4), 873. Doi: 10.3390/molecules25040873
Saldamlı, İ., & Temiz, A. (2014). Amino asitler, Peptitler, Proteinler. İlbilge Saldamlı (Ed.), Gıda Kimyası içinde (s. 227-315). Ankara: Hacettepe Üniversitesi Hastaneleri Basımevi
Sim, S. Y., Karwe, M. V., & Moraru, C. I. (2019) High pressure structuring of pea protein concentrates. Journal of Food Process Engineering, 42 (7), e13261. Doi: 10.1111/jfpe.13261
Soroka, W. (2009). Fundamentals of Packaging Technology. USA: Institute of Packaging Professionals
Toews, R., & Wang, N. (2013) Physicochemical and functional properties of protein concentrates from pulses. Food Research International, 52 (2), 445–451. Doi: 10.1016/j.foodres.2012.12.009
Yang, J., & Powers, J. R. (2016). Effects of High Pressure on Food Proteins. V. M. Balasubramaniam, G. V. Barbosa-Cánovas, H. L.M. Lelieveld (Eds.), In High Pressure Processing of Food. New York, NY: Springer
Zhang, X., Qi, J. R., Li, K. K., et al. (2012) Characterization of soy β-conglycinin–dextran conjugate prepared by Maillard reaction in crowded liquid system. Food Research International, 49 (2), 648–654. Doi: 10.1016/j.foodres.2012.09.001
Zhao, J., Tian, Z., & Chen, L. (2010) Effects of deamidation on structure and functional properties of barley hordein. Journal of Agricultural and Food Chemistry, 58 (21), 11448–11455. Doi: 10.1021/jf102307f
Zink, J., Wyrobnik, T., Prinz, T., et al. (2016) Physical, chemical and biochemical modifications of protein-based films and coatings: An extensive review. International Journal of Molecular Sciences, 17 (9), 1376. Doi: 10.3390/ijms17091376
Referanslar
Akharume, F. U., Aluko, R. E., & Adedeji, A. A. (2021) Modification of plant proteins for improved functionality: A review. Comprehensive Reviews in Food Science and Food Safety, 20, 198-224. Doi: 10.1111/1541-4337.12688
Akyüz, A., & Ersus-Bilek S. (2018) Protein Çöktürme Yöntemlerinin Karşılaştırılması. Çukurova Tarım ve Gıda Bilimleri Dergisi, 33 (2), 83-92.
Alonso-Miravalles, L., Jeske, S., Bez, J., et al. (2019) Membrane filtration and isoelectric precipitation technological approaches for the preparation of novel, functional and sustainable protein isolate from lentils. European Food Research and Technology, 245, 1855–1869. Doi: 10.1007/ s00217-019-03296-y
Belitz, H. D., Grosch, W., & Schieberle, P. (2009) Food Chemistry. Almanya: Springer
Ben-Harb, S., Panouillé, M., Huc-Mathis, D., et al. (2018). The rheological and microstructural properties of pea, milk, mixed pea/milk gels and gelled emulsions designed by thermal, acid, and enzyme treatments. Food Hydrocolloids, 77, 75-84. Doi: 10.1016/j.foodhyd.2017.09.022
Cabra, V., Arreguin, R., Vazquez-Duhalt, R., et al. (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. Doi: 10.1021/jf061002r
Chmielewska, A., Kozłowska, M., Rachwał, D., et al. (2021) Canola/rapeseed protein–nutritional value, functionality and food application: A review. Critical Reviews in Food Science and Nutrition, 61 (22), 3836–3856. Doi: 10.1080/10408398.2020.1809342
Choe, U., Lan, Y., Chen, B., et al. (2022) Structural, and functional properties of phosphorylated pea protein isolate by simplified co-spray drying process. Food Chemistry, 393 (1), 133441. Doi: 10.1016/j.foodchem.2022.133441
Onwulata, C. I., Konstance, R. P., Cooke, P.H., et al. (2003) Functionality of extrusion-texturized whey proteins. Journal of Dairy Science, 86, 3775–3782. Doi: 10.3168/jds.S0022-0302(03)73984-8
Demirci, M. (2006). Gıda Kimyası. Tekirdağ: Kelebek Matbaacılık
Dong, S., Gao, A., Zhao, Y., et al. (2017) Characterization of physicochemical and structural properties of atmospheric cold plasma (acp) modified zein. Food and Bioproducts Processing, 106, 65–74. Doi: 10.1016/j.fbp.2017.05.011
Eckert, E., Han, J., Swallow, K., et al. (2019) Effects of enzymatic hydrolysis and ultrafiltration on physicochemical and functional properties of faba bean protein. Cereal Chemistry, 96 (4), 725–741. Doi: 10.1002/cche.10169
Fernando, S. (2022) Pulse protein ingredient modification. Journal of the Science of Food and Agriculture, 102, 892-897. Doi: 10.1002/jsfa.11548
Flores, I., Cabra, V., Quirasco, M. C., et al. (2010) Emulsifying properties of chemically deamidated corn (zea mays) gluten meal. Food Science and Technology International, 16 (3), 241–250. Doi: 10.1177/1082013210366750
Glusac, J., Isaschar-Ovdat, S., & Fishman, A. (2020) Transglutaminase modifies the physical stability and digestibility of chickpea protein-stabilized oil-in-water emulsions. Food Chemistry, 315, 126301. Doi: 10.1016/j.foodchem.2020.126301
Hu, H., Cheung, I. W., Pan, S., et al. (2015) Effect of high intensity ultrasound on physicochemical and functional properties of aggregated soybean β-conglycinin and glycinin. Food Hydrocolloids, 45, 102-110. Doi: 10.1016/j.foodhyd.2014.11.004
Hu, Y., Du, L., Sun, Y., et al. (2023) Recent developments in phosphorylation modification on food proteins: Structure characterization, site identification and function. Food Hydrocolloids, 137, 108390. Doi: 10.1016/j.foodhyd.2022.108390
Jiang, L., Wang, J., Li, Y., et al. (2014) Effects of ultrasound on the structure and physical properties of black bean protein isolates. Food Research International, 62, 595–601. Doi: 10.1016/j.foodres.2014.04.022,
Kandemir, H., Aydın-Kandemir, F., Güler, B., et al. (2021) Soğuk Plazma Teknolojisi ve Tarımdaki Çeşitli Uygulama Alanları. Bursa Uludağ Üniversitesi Ziraat Fakültesi Dergisi, 35 (1), 217-245.
Khan, N. M., Mu, T. H., Sun, H. N., et al. (2015) Effects of high hydrostatic pressure on secondary structure and emulsifying behavior of sweet potato protein. High Pressure Research, 35 (2), 189-202. Doi: 10.1080/08957959.2015.1005013
Kumar, M., Tomar, M., Punia, S., et al. (2022) Plant-based proteins and their multifaceted industrial applications. LWT, 154, 112620. Doi: 10.1016/j.lwt.2021.112620
Lin, S., Huff, H., & Hsieh, F. (2000) Texture and chemical characteristics of soy protein meat analog extruded at high moisture. Journal of Food Science, 65 (2), 264–269. Doi: 10.1111/j.1365-2621.2000.tb15991.x
Ma, Z., Boye, J. I., Simpson, B. K., et al. (2011) Thermal processing effects on the functional properties and microstructure of lentil, chickpea, and pea flours. Food Research International, 44 (8), 2534–2544. Doi: 10.1016/j.foodres.2010.12.017
Martínez-Velasco, A., Lobato-Calleros, C., Hernández-Rodríguez, B. E., et al. (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. Doi: 10.1016/j.ultsonch.2018.02.007
Meganaharshini, M., Sudhakar, V., Dhivya-Bharathi, N., et al. (2023) Review on recent trends in the application of protein concentrates and isolates – A food industry perspective. Food and Humanity, 1, 308-325. Doi:10.1016/j.foohum.2023.05.022
Mehenktaş, C. Süt İşlemede Ultrason Kullanımı. (2022) Akademik Gıda, 20 (4), 474-481.
Messens, W., Van Camp, J., & Huyghebaert, A. (1997) The use of high pressure to modify the functionality of food proteins. Trends in Food Science & Technology, 8 (4), 107–112. Doi: 10.1016/S0924-2244(97)01015-7
Oliveira, F. C. D., Coimbra, J. S. D. R., Oliveira, E. B. D., et al. (2016) Food protein-polysaccharide conjugates obtained via the Maillard reaction: a review. Critical Reviews in Food Science and Nutrition, 56, 1108–1125. Doi: 10.1080/10408398.2012.755669
Ötleş, S., Özdestan-Ocak, Ö., Nakilcioğlu, E., Kartal, C., & Özyurt, V. H. (2015). Gıda Kimyası. İzmir: Ege Üniversitesi Basımevi
Phongthai, S., D’Amico, S., Schoenlechner, R., et al. (2016) Comparative study of rice bran protein concentrate and egg albumin on gluten-free bread properties. Journal of Cereal Science, 72, 38–45. Doi: 10.1016/j.jcs.2016.09.015
Phongthai, S., Lim, S. T., & Rawdkuen, S. (2016) Optimization of microwave-assisted extraction of rice bran protein and its hydrolysates properties. Journal of Cereal Science, 70, 146-154. Doi: 10.1016/j.jcs.2016.06.001
Rasheed, F., Markgren, J., Hedenqvist, M., et al. (2020) Modeling to understand plant protein structure-function relationships-Implications for seed storage proteins. Molecules, 25 (4), 873. Doi: 10.3390/molecules25040873
Saldamlı, İ., & Temiz, A. (2014). Amino asitler, Peptitler, Proteinler. İlbilge Saldamlı (Ed.), Gıda Kimyası içinde (s. 227-315). Ankara: Hacettepe Üniversitesi Hastaneleri Basımevi
Sim, S. Y., Karwe, M. V., & Moraru, C. I. (2019) High pressure structuring of pea protein concentrates. Journal of Food Process Engineering, 42 (7), e13261. Doi: 10.1111/jfpe.13261
Soroka, W. (2009). Fundamentals of Packaging Technology. USA: Institute of Packaging Professionals
Toews, R., & Wang, N. (2013) Physicochemical and functional properties of protein concentrates from pulses. Food Research International, 52 (2), 445–451. Doi: 10.1016/j.foodres.2012.12.009
Yang, J., & Powers, J. R. (2016). Effects of High Pressure on Food Proteins. V. M. Balasubramaniam, G. V. Barbosa-Cánovas, H. L.M. Lelieveld (Eds.), In High Pressure Processing of Food. New York, NY: Springer
Zhang, X., Qi, J. R., Li, K. K., et al. (2012) Characterization of soy β-conglycinin–dextran conjugate prepared by Maillard reaction in crowded liquid system. Food Research International, 49 (2), 648–654. Doi: 10.1016/j.foodres.2012.09.001
Zhao, J., Tian, Z., & Chen, L. (2010) Effects of deamidation on structure and functional properties of barley hordein. Journal of Agricultural and Food Chemistry, 58 (21), 11448–11455. Doi: 10.1021/jf102307f
Zink, J., Wyrobnik, T., Prinz, T., et al. (2016) Physical, chemical and biochemical modifications of protein-based films and coatings: An extensive review. International Journal of Molecular Sciences, 17 (9), 1376. Doi: 10.3390/ijms17091376
