A novel multi-biofunctional protein from brown rice hydrolysed by endo/endo-exoproteases

Food & Function Pub Date: 2016-05-09 DOI: 10.1039/C5FO01344E

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.

Graphical abstract: A novel multi-biofunctional protein from brown rice hydrolysed by endo/endo-exoproteases
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