期刊
JOURNAL OF FUNCTIONAL FOODS
卷 6, 期 -, 页码 462-469出版社
ELSEVIER
DOI: 10.1016/j.jff.2013.11.012
关键词
Peptic hydrolysis; Whey protein; Cross-linking; Transglutaminase; Desolvation; Ferric reducing antioxidant power
资金
- Iran National Science Foundation (INSF)
- University of Tehran
- Center of Excellence for Application of Modern Technologies in Production of Functional Foods and Drinks
Whey proteins were hydrolyzed with pepsin to antioxidant peptides, cross-linked by transglutaminase and then particulated through ethanol addition. Reducing power assay indicated that cross-linking enhanced the antioxidant activity of hydrolysate. Particles prepared from non-hydrolyzed protein, peptides and cross-linked peptides were all of bimodal size distribution comprised from sub-micron (>100 nm) and nanoscalar (<100 nm) populations. The enzymatic cross-linking resulted in generation of more monodisperse particles and increased the volume fraction of nano-sized population. Scanning electron microscopy revealed an almost spherical morphology for samples and Fourier transform infrared spectroscopy confirmed the cross-linking of peptides. Heat-scanning of samples by a differential scanning calorimeter indicated that cross-linking did not affect the thermal behavior of particles. However, a reinforcing effect on particles was suggested for cross-linking based on the in vitro tests carried out at various digestion media. Crosslinking slowed down the release rate of entrapped caffeine from particles in a simulated gastric fluid. (C) 2013 Elsevier Ltd. All rights reserved.
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