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Journal of Food Science and Technology

, Volume 56, Issue 11, pp 5116–5127 | Cite as

Effect of protein aggregates on properties and structure of rice bran protein-based film at different pH

  • Na Wang
  • Ahmed S. M. Saleh
  • Yuzhe Gao
  • Peng Wang
  • Yumin DuanEmail author
  • Zhigang XiaoEmail author
Original Article

Abstract

Rice bran protein (RBP) aggregates were prepared by heating of RBP solution at 90 °C for 4 h at pH 2, 7, or 11 and used for preparing of packaging films. The structure and properties of RBP aggregates and RBP-based films were characterized with sodium dodecyl sulfate–polyacrylamide gel electrophoresis, transmission electron microscopy, scanning electron microscope, differential scanning calorimetry, Fourier transform infrared spectroscopy and circular dichroism. The results showed formation of fibrillar, globular, and large molecular protein aggregates during the heating at pH 2, 7 and 11. The heat-aggregated RBP-based films exhibited lower opacity, moisture content, water solubility, and water vapor permeability than those of untreated RBP-based films. Also, improved mechanical and thermal properties were found for the heat-aggregated RBP-based films. In addition, the heat-aggregated RBP-based film at pH 11 showed homogenous and smooth surface as well as compact appearance compared with the untreated RBP-based films or heat-aggregated RBP-based film at pH 2 or 7. Furthermore, the secondary structure of heat-aggregated RBP film exhibited an increase in β-sheet content and molecular interactions through non-covalent bonds. The obtained results indicated that formation of protein aggregates could improve physical, mechanical, and thermal properties of RBP-based film, especially at pH 11.

Keywords

Rice bran protein Protein aggregates Packaging film pH 

Notes

Acknowledgements

This work was supported by the Chinese Ministry of Science and Technology within Talented Young Scientist Program (EG-16-004) and the National Key R&D Program of China (2018YFD0401003).

References

  1. Adebiyi AP, Adebiyi AO, Jin D-H, Ogawa T, Muramoto K (2008) Rice bran protein-based edible films. Int J Food Sci Technol 43:476–483.  https://doi.org/10.1111/j.1365-2621.2006.01475.x CrossRefGoogle Scholar
  2. Adebiyi AP, Adebiyi AO, Hasegawa Y, Ogawa T, Muramoto K (2009) Isolation and characterization of protein fractions from deoiled rice bran. Eur Food Res Technol 228:391–401.  https://doi.org/10.1007/s00217-008-0945-4 CrossRefGoogle Scholar
  3. Ainis WN, Ersch C, Ipsen R (2018) Partial replacement of whey proteins by rapeseed proteins in heat-induced gelled systems: effect of pH. Food Hydrocoll 77:397–406.  https://doi.org/10.1016/j.foodhyd.2017.10.016 CrossRefGoogle Scholar
  4. Akkermans C, van der Goot AJ, Venema P, van der Linden E, Boom RM (2008) Formation of fibrillar whey protein aggregates: influence of heat and shear treatment, and resulting rheology. Food Hydrocoll 22:1315–1325.  https://doi.org/10.1016/j.foodhyd.2007.07.001 CrossRefGoogle Scholar
  5. ASTM (2001) Standard test method for tensile properties of thin plastic sheeting. In: Standard designations D882-01. annual book of ASTM standards. American Society for Testing and Materials, PhiladelphiaGoogle Scholar
  6. ASTM (2014) Standard test method for water vapor transmission of materials. In: Standard designations E96/E96M. annual book of ASTM standards. American Society for Testing and Materials, PhiladelphiaGoogle Scholar
  7. Barth A (2007) Infrared spectroscopy of proteins. Biochim Biophys Acta 1767:1073–1101.  https://doi.org/10.1016/j.bbabio.2007.06.004 CrossRefPubMedGoogle Scholar
  8. Bolder SG, Hendrickx H, Sagis LMC, van der Linden E (2006) Fibril assemblies in aqueous whey protein mixtures. J Agric Food Chem 54:4229–4234.  https://doi.org/10.1021/jf060606s CrossRefPubMedGoogle Scholar
  9. Fan L, Ge A, Chen XD, Mercadé-Prieto R (2019) The role of non-covalent interactions in the alkaline dissolution of heat-set whey protein hydrogels made at gelation pH 2–11. Food Hydrocoll 89:100–110.  https://doi.org/10.1016/j.foodhyd.2018.10.035 CrossRefGoogle Scholar
  10. Gao Y-Z, Xu H-H, Ju T-T, Zhao X-H (2013) The effect of limited proteolysis by different proteases on the formation of whey protein fibrils. J Dairy Sci 96:7383–7392.  https://doi.org/10.3168/jds.2013-6843 CrossRefPubMedGoogle Scholar
  11. Gnanasambandam R, Hettiarachchy N, Coleman M (2006) Mechanical and barrier properties of rice bran films. J Food Sci 62:395–398.  https://doi.org/10.1111/j.1365-2621.1997.tb04009.x CrossRefGoogle Scholar
  12. Gu L, Wang M, Zhou J (2013) Effects of protein interactions on properties and microstructure of zein–gliadin composite films. J Food Eng 119:288–298.  https://doi.org/10.1016/j.jfoodeng.2013.05.022 CrossRefGoogle Scholar
  13. Hoque MS, Benjakul S, Prodpran T, Songtipya P (2011) Properties of blend film based on cuttlefish (Sepia pharaonis) skin gelatin and mungbean protein isolate. Int J Biol Macromol 49:663–673.  https://doi.org/10.1016/j.ijbiomac.2011.06.028 CrossRefPubMedGoogle Scholar
  14. Johnson WC Jr (1990) Protein secondary structure and circular dichroism: a practical guide. Proteins 7:205–214.  https://doi.org/10.1002/prot.340070302 CrossRefPubMedGoogle Scholar
  15. Kaewprachu P, Osako K, Rawdkuen S (2018) Effects of plasticizers on the properties of fish myofibrillar protein film. J Food Sci Technol 55:3046–3055.  https://doi.org/10.1007/s13197-018-3226-7 CrossRefPubMedPubMedCentralGoogle Scholar
  16. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685.  https://doi.org/10.1038/227680a0 CrossRefPubMedGoogle Scholar
  17. Liang J, Yan H, Zhang J-Y, Dai W-Z, Gao X-L, Zhou Y-B, Wan X-C, Puligundla P (2017) Preparation and characterization of antioxidant edible chitosan films incorporated with epigallocatechin gallate nanocapsules. Carbohydr Polym 171:300–306.  https://doi.org/10.1016/j.carbpol.2017.04.081 CrossRefPubMedGoogle Scholar
  18. Liu J, Liu S, Wu Q, Gu Y, Kan J, Jin C (2017) Effect of protocatechuic acid incorporation on the physical, mechanical, structural and antioxidant properties of chitosan film. Food Hydrocoll 73:90–100.  https://doi.org/10.1016/j.foodhyd.2017.06.035 CrossRefGoogle Scholar
  19. Loveday SM, Anema SG, Singh H (2017) β-Lactoglobulin nanofibrils: the long and the short of it. Int Dairy J 67:35–45.  https://doi.org/10.1016/j.idairyj.2016.09.011 CrossRefGoogle Scholar
  20. Otoni CG, Avena-Bustillos RJ, Olsen CW, Bilbao-Sainz C, McHugh TH (2016) Mechanical and water barrier properties of isolated soy protein composite edible films as affected by carvacrol and cinnamaldehyde micro and nanoemulsions. Food Hydrocoll 57:72–79.  https://doi.org/10.1016/j.foodhyd.2016.01.012 CrossRefGoogle Scholar
  21. Perera SP, McIntosh TC, Wanasundara JPD (2016) Structural properties of cruciferin and napin of Brassica napus (Canola) show distinct responses to changes in pH and temperature. Plants Basel.  https://doi.org/10.3390/plants5030036 CrossRefPubMedPubMedCentralGoogle Scholar
  22. Reiting R, Grohmann L, Moris G, Maede D (2013) Detection and characterization of an unknown rice event in Basmati rice products. Eur Food Res Technol 236:715–723.  https://doi.org/10.1007/s00217-013-1928-7 CrossRefGoogle Scholar
  23. Schmidt CG, Cerqueira MA, Vicente AA, Teixeira JA, Furlong EB (2015) Rice bran protein-based films enriched by phenolic extract of fermented rice bran and montmorillonite clay. Cyta J Food 13:204–212.  https://doi.org/10.1080/19476337.2014.939998 CrossRefGoogle Scholar
  24. Sharma L, Singh C (2016) Sesame protein based edible films: development and characterization. Food Hydrocoll 61:139–147.  https://doi.org/10.1016/j.foodhyd.2016.05.007 CrossRefGoogle Scholar
  25. Shimada K, Cheftel JC (1988) Texture characteristics, protein solubility, and sulfhydryl group/disulfide bond contents of heat-induced gels of whey protein isolate. J Agric Food Chem 36:1018–1025.  https://doi.org/10.1021/jf00083a029 CrossRefGoogle Scholar
  26. Shin YJ, Jang S-A, Song KB (2011) Preparation and mechanical properties of rice bran protein composite films containing gelatin or red algae. Food Sci Biotechnol 20:703–707.  https://doi.org/10.1007/s10068-011-0099-1 CrossRefGoogle Scholar
  27. Shun-Tang G, Ono T, Mikami M (1997) Interaction between protein and lipid in soybean milk at elevated temperature. J Agric Food Chem 45:4601–4605.  https://doi.org/10.1021/jf970417x CrossRefGoogle Scholar
  28. Tulamandi S, Rangarajan V, Rizvi SSH, Singhal RS, Chattopadhyay SK, Saha NC (2016) A biodegradable and edible packaging film based on papaya puree, gelatin, and defatted soy protein. Food Packag Shelf Life 10:60–71.  https://doi.org/10.1016/j.fpsl.2016.10.007 CrossRefGoogle Scholar
  29. Wang N, Gao Y-Z, Wang P, Yang S, Xie T-M, Xiao Z-G (2016) Effect of microwave modification on mechanical properties and structural characteristics of soy protein isolate and zein blended film. Czech J Food Sci 34:180–188.  https://doi.org/10.17221/442/2015-cjfs CrossRefGoogle Scholar
  30. Wang R, Liu J, Guo S (2018) Binding of phytate to soybean protein during the heat treatment of soymilk and its effect on protein aggregation. Food Hydrocoll 84:368–378.  https://doi.org/10.1016/j.foodhyd.2018.06.031 CrossRefGoogle Scholar
  31. Whitmore L, Wallace BA (2008) Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89:392–400.  https://doi.org/10.1002/bip.20853 CrossRefPubMedGoogle Scholar
  32. Zadeh EM, O’Keefe SF, Kim YT, Cho JH (2018) Evaluation of enzymatically modified soy protein isolate film forming solution and film at different manufacturing conditions. J Food Sci 83:946–955.  https://doi.org/10.1111/1750-3841.14018 CrossRefGoogle Scholar
  33. Zhang Y-H, Huang L-H (2014) Effect of heat-induced formation of rice bran protein fibrils on morphological structure and physicochemical properties in solutions and gels. Food Sci Biotechnol 23:1417–1423.  https://doi.org/10.1007/s10068-014-0194-1 CrossRefGoogle Scholar
  34. Zhang J, Zhang H, Wang L, Guo X, Wang X, Yao H (2010) Isolation and identification of antioxidative peptides from rice endosperm protein enzymatic hydrolysate by consecutive chromatography and MALDI-TOF/TOF MS/MS. Food Chem 119:226–234.  https://doi.org/10.1016/j.foodchem.2009.06.015 CrossRefGoogle Scholar
  35. Zhang Y-H, Huang L-H, Wei Z-C (2014) Effects of additional fibrils on structural and rheological properties of rice bran albumin solution and gel. Eur Food Res Technol 239:971–978.  https://doi.org/10.1007/s00217-014-2294-9 CrossRefGoogle Scholar

Copyright information

© Association of Food Scientists & Technologists (India) 2019

Authors and Affiliations

  1. 1.College of FoodShenyang Agricultural UniversityShenyangChina
  2. 2.College of Grain Science and TechnologyShenyang Normal UniversityShenyangChina
  3. 3.Department of Food Science and Technology, Faculty of AgricultureAssiut UniversityAssiutEgypt

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