Functional properties of enzymatic hydrolysate and peptide fractions from perilla seed meal protein

• Autorzy: Pork B.Y. , Yoon K.Y.
• Języki publikacji: EN

Abstrakty

EN

The present study aimed to decompose perilla seed meal (PSM) proteins via enzymatic degradation and to evaluate the functional properties of the resulting enzymatic hydrolysate and peptide fractions for the utilization of PSM, a by-product in the production of perilla seed oil. PSM protein hydrolysate was fractionated based on molecular weight using an ultra ltration system, and the physical properties required to utilize the hydrolysate and peptide fractions as functional food components were determined. The enzymatic hydrolysate and peptide fractions showed higher solubility, oil absorption capacity, and emulsifying and foaming properties than protein isolates. In particular, peptide fractions below the 5 kDa showed high solubility, emulsifying activity, and foaming capacity. Therefore, these peptide fractions are ideal as functional raw materials and substitutes that can be used to improve the quality of various processed food products and protein supplements.

• Wydawca: -
• Czasopismo: Polish Journal of Food and Nutrition Sciences
• Rocznik: 2019
• Tom: 69
• Numer: 2
• Opis fizyczny: p.119-127,ref.

Twórcy

autor

Pork B.Y.

• Department of Food and Nutrition, Yeungnam University, Gyeongsan, Gyeongbuk 38547, Korea

autor

Yoon K.Y.

• Department of Food and Nutrition, Yeungnam University, Gyeongsan, Gyeongbuk 38547, Korea

Bibliografia

• 1. Adebowale, K.O., Lawal, O.S. (2003). Foaming, gelation and electrophoretic characteristics of mucana bean (Mucan pruriens) protein concentrates. Food Chemistry, 83(2), 237-246.
• 2. Bang, B.H., Seo, J.S., Jeon, E.J., Kim, K.P. (1996). Foaming capacity and foaming stability of protein recovered from red crab processing water. Korean Journal of Food Nutrition, 9(3), 325-330.
• 3. Benítez, R., Ibarz, A., Pagan, J. (2008). Protein hydrolysates: processes and applications. Acta Bioquí mica Clínica Latinoamericana, 42(2), 227-236.
• 4. Beuchat, L.R. (1977). Functional and electrophoretic characteristics of succinylated peanut our proteins. Journal of Agricultural and Food Chemistry, 25(2), 258-261.
• 5. Bhattacharjee, S., Sultana, A., Sazzad, M.H., Islam, M.A., Ahtashom M.M., Asaduzzaman (2013). Analysis of the proximate composition and energy values of two varieties of onion (Allium cepa L.) bulbs of different origin: A comparative study. International Journal of Nutrition and Food Sciences, 2(5), 246-253.
• 6. Cabra, V., Arreguín, R., Farres, A. (2008). Emulsifying properties of proteins. Boletín de la Sociedad Química de México, 2(2), 80-89.
• 7. Chalamaiah, M., Dinesh Kumar, B., Hemalatha, R., Jyothirmayi, T. (2012). Fish protein hydrolysates: Proximate composition, amino acid composition, antioxidant activities and applications: A review. Food Chemistry, 135(4), 3020-3038.
• 8. Chove, B.E., Grandison, A.S., Lewis, M.J. (2002). Emulsifying properties of soy protein isolates obtained by micro ltration. Journal of the Science of Food and Agriculture, 82(3), 267-272.
• 9. Córdova-Murueta, J.H., García-Carreño, F.L. (2002). Nutritive value of squid and hydrolyzed protein supplement in shrimp feed. Aquaculture, 210(1), 371-384.
• 10. Crenwelge, D.D., Dill, P., Tybor, P., Landmann, L.A. (1974). A comparison of the emulsi cation capacities of some protein concentrates. Journal of Food Science, 39(1), 175-177.
• 11. Dehnad, D., Jafari, S.M., Afrasiabi, M. (2016). In uence of drying on functional properties of food biopolymers: From traditional to novel dehydration techniques. Trends in Food Science & Technology, 57, 116-131.
• 12. Di Bernardini, R., Harnedy, P., Bolton, D., Kerry, J., OijNeill, E., Mullen, A.M., Hayes, M. (2011). Antioxidant and antimicrobial peptidic hydrolysates from muscle protein sources and by-products. Food Chemistry, 124(4), 1296-1307.
• 13. Eldridge, A.C., Hall, P.K., Wolf, W.J. (1963). Stable foams from unhydrolyzed soybean protein. Food Technology, 17, 1592-1595
• 14. Gnanasambandam, R., Hettiarachchy, N.S. (1995). Protein concentrates from unstabilized and stabilized rice bran: preparation and properties. Journal of Food Science, 60(5), 1066-1069, 1074.
• 15. Hermansson, A.M.J. (1975). Functional properties of proteins for food- ow properties. Journal of Texture Studies, 5(4), 425-439.
• 16. Jang, H.R., Liceaga, A.M., Yoon, K.Y. (2016). Puri cation, characterisation and stability of an antioxidant peptide derived from sand sh (Arctoscopus japonicus) protein hydrolysates. Journal of Functional Foods, 20, 433-442
• 17. Kim, C.H., Ahn, M.S. (2007). Pysicochemical properties of whey protein isolate. Korean Journal of Food Science and Technology, 39(1), 50-54.
• 18. Kimatu, B.M.K., Zhao, L., Biao, Y. Ma, C., Yang, W., Pei, F., Hu, Q. (2017). Antioxidant potential of edible mushroom (Agaricus bisporus) protein hydrolysates and their ultra ltration fractions. Food Chemistry, 230(1), 58-67.
• 19. Kinsella, J.E. (1979). Functional properties of soy proteins. Journal of the American Oil Chemistsij Society, 56(3), 242-258.
• 20. Kinsella, J.E., Melachouris, N. (1976). Functional properties of proteins in foods: a survey. Critical Reviews in Food Science and Nutrition, 7(3), 219-280.
• 21. Klompong, V., Benjakul, S., Kantachote, D., Shahidi, F. (2017). Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as in uenced by the degree of hydrolysis and enzyme type. Food Chemistry, 102(4), 1317-1327.
• 22. Lee, S.H., Cho, Y.J., Chun, S.S., Kim, Y.H., Choi, S. (1995). Functional properties of proteolytic enzyme-modi ed isolated sesame meal protein. Korean Journal of Food Science and Technology, 27(5), 708-715.
• 23. Lee, Y.I. (2015). Manufacturing soy-protein concentrates and isolates by membrane technology. International Journal of Agriculture Innovations and Research, 3(4), 1150-1158.
• 24. Lui, F.K., Nie, Y.H., Shen, B.Y. (1988). Manufacturing soy protein isolate by ultra ltration. Proceedings of the World Congress on Vegetable Protein Utilization in Human Foods and Animal Feedstuffs. Singapore, October 1988, American Oil Chemistsij Society, Champaign, IL, pp. 84-90.
• 25. Manak, L.T., Lawhon, J.T., Lusas, E.W. (1980). Functional potential of soy, cottonseed, and peanut protein isolates produced by industrial membrane systems. Journal of Food Science, 45(2), 236-238.
• 26. Megías, C., Pedroche, J., Yust, M.M., Alaiz, M., Girón-Calle, J., Millán, F., Vioque, J. (2009). Sun ower protein hydrolysates reduce cholesterol micellar solubility. Plant Foods Human Nutrition,64(2), 86-93.
• 27. Meng, L., Lozano, Y., Bombarda, I., Gaydou, E.M., Li, B. (2009a). Polyphenol extraction from eight Perilla frutescens culivars. Comptes Rendus Chimie, 12(5), 602-611.
• 28. Meng, L., Lozano, Y., Bombarda, I., Gaydou, E.M., Li, B. (2009b). Antioxidant activities of polyphenols extracted from Perilla frutescens varieties. Molecules, 14(1), 133-140.
• 29. Mohammad, A. (2011). Health effects of omega-3,6,9 fatty acids: Perilla frutescens is a good example of plant oils. OrientalPharmacy and Experimental Medicine, 11(1), 51-59.
• 30. Mutilangi, W.A.M., Panyam, D., Kilara, A. (1996). Functional properties of hydrolysates from proteolysis of heat-denatured whey protein isolate. Journal of Food Science, 61(2), 270-275.
• 31. Nalinanon, S., Benjakul, S., Kishimura, H., Shahidi, F. (2011). Functionalities and antioxidant properties of protein hydrolysates from the muscle of ornate thread n bream treated with pepsin skipjack tuna. Food Chemistry, 124(4), 1354-1362.
• 32. Nguyen, E., Jones, O., Kim, Y.H.B., Martin-Gonzalez, S., Liceaga, A.M. (2017). Impact of microwave-assisted enzymatic hydrolysis on functional and antioxidant properties of rainbow trout Oncorhynchus mykiss by-products. Fisheries Science, 83(2), 317-331.
• 33. Park, B.Y., Yoon, K.Y. (2018). Conditions for hydrolysis of perilla seed meal protein for producing hydrolysates and ultra ltered peptides and their antioxidant activity. Korean Journal of Food Preservation, 25(5), 605-612.
• 34. Park, J.Y., Yoon K.Y. (2014). Comparison of the nutrient composition and quality of the root of Allium hookeri grown in Korea and Myanmar. Korean Journal of Food Science and Technology, 45(5), 544-548.
• 35. Pearson, A.M. (1994). Soy proteins. In Nakamura (Ed.), Developments in Food Engineering. Blackie Academic & Professional Publishing Co. London, U.K. pp. 67-104.
• 36. Sarabandi, K., Mahoonak, A.S., Hamishekar, H., Ghorbni, M., Jafari, S.M. (2018). Microencapsulation of casein hydrolysates: Physicochemical, antioxidant and microstructure properties. Journal of Food Engineering, 237, 86-95.
• 37. Sathe, S.K., Salunkhe, D.K. (1981). Functional properties of the great northern bean (Phaseolus vulgaris L.) proteins: emulsion, foaming, viscosity, and gelation properties. Journal of Food Science, 46(1), 71-81.
• 38. Schmidl, M.K., Taylor, S.L., Nordlee J.A. (1994). Use of hydrolysate-based products in special medical diets. Food Technology, 48(10), 77-85.
• 39. Singh, N., Kaur, M., Sandhu, K.S. (2005). Physicochemical and functional properties of freeze-dried and oven dried corn gluten meals. Drying Technology, 23(4), 975-988.
• 40. Tan, E.S., Ngoh, Y.Y., Gan, C.Y. (2014). A comparative study of physicochemical characteristics and functionalities of pinto bean protein isolate (PBPI) against the soybean protein isolate (SPI) after the extraction optimization. Food Chemistry, 152(1),447-455.
• 41. Townsend, A.A., Nakai, S. (1983). Relationships between hydrophobicity and foaming characteristics of food proteins. Journal of Food Science, 48(2), 588-594.
• 42. Wierenga, P., Gruppen, H. (2010). New views on foams from protein solutions. Current Opinion in Colloid & Interface Science, 15(5), 365-373.
• 43. Wu, W.U., Hettiarachchy, N.S., Qi, M. (1998). Hydrophobicity, solubility, and emulsifying properties of soy protein peptides prepared by papain modi cation and ultra ltration. Journal of the American Oil Chemistsij Society, 75(7), 845-850.
• 44. Yim, M.H., Lee, J.H. (2000). Functional properties of fractionated soy protein isolates by protease from Meju. Food Science and Biotechnology, 9(4), 253-257.

Identyfikatory

DOI

10.31883/pjfns-2019-0011