The Effect of Rapeseed Protein Structural Modification on Microstructural Properties of Peptide Microcapsules
- 505 Downloads
This study investigated the chemical, enzymatic, and physical modifications of rapeseed protein isolate (RPI) to improve its mechanical properties for its use as wall materials for rapeseed peptide (RP) microencapsulation by spray drying. The objective was to determine the effect of protein modification and the influence of the core/shell ratio on microcapsule properties. Results obtained demonstrated that microcapsules derived from the hydrolysis of RPI as wall material showed lower encapsulation efficiency (NE) than the native RPI microcapsules (63 ± 1.0–84 ± 1.7 and 91.4 ± 1.4 %, respectively). Conversely, acylated (degree of acylation (DA) of 47 %) and high pressure (HP) 400 MPa treatment of RPI as wall materials allowed a higher NE to be up to 99 ± 2.2 and 94 ± 1.3 %, respectively. Moreover, the data of the IR spectra curve fitting showed that wall materials obtained from hydrolyzed RPI resulted in greater loss of total secondary structures when compared to the wall material from acylated, HP-treated, and native RPI. Nanomechanical experiments also indicated that the microcapsules from hydrolyzed RPI underwent remarkable softening with an associated drop in Young’s modulus value (245 MPa) when compared to microcapsules with acylated and HP-treated RPI (450 and 310 MPa, respectively). The above results suggested that there might be an excellent correlation between IR spectra curve fittings and the nanomechanical data depicting the microstructural properties of microcapsules. In addition, higher microcapsule size and NE were observed while decreasing the spray-drying yield as the RP concentration was increased.
KeywordsMicrocapsules Rapeseed protein isolate Acylation Hydrolysis High pressure Mechanical characterization
Funding for this work was provided through the Agricultural Science and Technology Innovation Capital of Jiangsu Province (project no. CX (13) 3088) and Universities Natural Science Research Project of Jiangsu Province (project no. 14KJ13550003). The authors acknowledge the financial support of the Natural Science Foundation of Jiangsu Province of China (BK20131435) and the Special Project of State Grain Industry (201413007).
- Adler-Nissen, J. (1986). Enzymic hydrolysis of food proteins. England: Elsevier.Google Scholar
- Dong, X. Y., Guo, L. L., Wei, F., Li, J. F., Jiang, M. L., Li, G. M., Zhao, Y. D., & Chen, H. (2011). Some characteristics and functional properties of rapeseed protein prepared by ultrasonication, ultrafiltration and isoelectric precipitation. Journal of the Science of Food and Agriculture, 91(8), 1488–1498.CrossRefGoogle Scholar
- Fleddermann, M., Fechner, A., Rößler, A., Bähr, M., Pastor, A., Liebert, F., & Jahreis, G. (2013). Nutritional evaluation of rapeseed protein compared to soy protein for quality, plasma amino acids, and nitrogen balance—a randomized cross-over intervention study in humans. Clinical Nutrition, 32, 519–526.CrossRefGoogle Scholar
- Gaonkar, A., Vasisht, N., Khare, A., & Sobel, R. (2014). Microencapsulation in the food industry: a practical implementation guide. Amsterdam: Elsevier.Google Scholar
- Karayannidou, A., Makri, E., Papalamprou, E., Doxastakis, G., Vaintraub, I., Lapteva, N., & Articov, G. (2007). Limited proteolysis as a tool for the improvement of the functionality of sunflower (Helianthus annus L.) protein isolates produced by seeds or industrial by-products (solvent cake). Food Chemistry, 104, 1728–1733.CrossRefGoogle Scholar
- Li, X.R. (2009). Microencapsulation properties of soy protein isolate. South China University of Technology, pp.16-17.Google Scholar
- Mateos-Aparicio, I., Redondo-Cuenca, A., Villanueva-Suárez, M., & Zapata-Revilla, M. (2008). Soybean, a promising health source. Nutrición Hospitalaria, 23, 305.Google Scholar
- Schwenke, K. (1994). Rapeseed proteins. New and developing sources of food proteins. Springer, pp. 281-306.Google Scholar
- Yin, S.-W., Tang, C.-H., Wen, Q.-B., Yang, X.-Q., & Yuan, D.-B. (2010). The relationships between physicochemical properties and conformational features of succinylated and acetylated kidney bean (Phaseolus vulgaris L.) protein isolates. Food Research International, 43, 730–738.CrossRefGoogle Scholar