A novel multi-biofunctional protein from brown rice hydrolysed by endo/endo-exoproteases
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Author list: Selamassakul O., Laohakunjit N., Kerdchoechuen O., Ratanakhanokchai K.
Publisher: Royal Society of Chemistry
Publication year: 2016
Journal: Food and Function (2042-6496)
Volume number: 7
Issue number: 6
Start page: 2635
End page: 2644
Number of pages: 10
ISSN: 2042-6496
eISSN: 2042-650X
Languages: English-Great Britain (EN-GB)
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Abstract
Brown rice, which is a less allergenic food grain and contains essential amino acids, was hydrolysed by bromelain and PROTEASE FP51® to improve its functionalities and taste for food applications. The hydrolysate prepared by bromelain (eb-RPH) had high protein solubility, surface hydrophobicity, low molecular weight peptides, hydrophobic amino acids (leucine, valine and glycine) and flavor amino acids (glutamic acid and aspartic acid). The eb-RPH exhibited higher 1,1-diphenyl-2-picrylhydrazyl (DPPH) and 2,2′-azino-bis 3-ethylbenzthiazoline-6-sulfonic (ABTS+) radical-scavenging activities of 76.62% and 52.96%, respectively, and possessed a better foaming capacity (221.76%) and emulsifying capacity (32.34%) than the hydrolysate prepared by PROTEASE FP51® (ep-RPH) did. The eb-RPH gave the desired taste, which is attributed to volatile flavor compounds (benzaldehyde, benzeneacetaldehyde and 2-acetyl-1-pyrroline) and non-volatile flavor compounds, such as monosodium glutamate, 5′-guanosine monophosphate and 5′-inosine monophosphate (0.07, 0.03 and 0.05 mg mL-1, respectively). Brown rice peptides generated by bromelain were novel bioactive peptides with multifunctional properties. © 2016 The Royal Society of Chemistry.
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