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. 2021 Jun 12;26(12):3605.
doi: 10.3390/molecules26123605.

Evaluating the Antioxidants, Whitening and Antiaging Properties of Rice Protein Hydrolysates

Hui-Ju Chen  1   2 , Fan-Jhen Dai  2 , Cheng-You Chen  3 , Siao-Ling Fan  2 , Ji-Hong Zheng  4 , Yu-Chun Huang  2 , Chi-Fai Chau  1 , Yung-Sheng Lin  3   4   5 , Chin-Shuh Chen  1
Affiliations

Evaluating the Antioxidants, Whitening and Antiaging Properties of Rice Protein Hydrolysates

Hui-Ju Chen et al. Molecules. .

Abstract

Plant-derived protein hydrolysates have potential applications in nutrition. Rice protein hydrolysates (RPHs), an excellent source of proteins, have attracted attention for the development of cosmeceuticals. However, few studies have reported the potential application of RPH in analysis, and this study examined their antioxidant activities and the inhibitory activities of skin aging enzymes. The results indicated that the total phenolic and flavonoid concentrations were 2.06 ± 0.13 mg gallic acid equivalent/g RPHs and 25.96 ± 0.52 µg quercetin equivalent/g RPHs, respectively. RPHs demonstrated dose-dependent activity for scavenging free radicals from 1,1-diphenyl-2-picrylhydrazyl [half-maximal inhibitory concentration (IC50) = 42.58 ± 2.1 mg/g RPHs] and 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (IC50 = 2.11 ± 0.88 mg/g RPHs), dose-dependent reduction capacity (6.95 ± 1.40 mg vitamin C equivalent/g RPHs) and oxygen radical absorbance capacity (473 µmol Trolox equivalent/g RPHs). The concentrations of the RPH solution required to achieve 50% inhibition of hyaluronidase and tyrosinase activities were determined to be 8.91 and 107.6 mg/mL, respectively. This study demonstrated that RPHs have antioxidant, antihyaluronidase, and antityrosinase activities for future cosmetic applications.

Keywords: antioxidant; cosmetic; hyaluronidase; rice protein hydrolysate; tyrosinase.

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Conflict of interest statement

The authors declare that there are no conflicts of interest.

Figures

Figure 1
Figure 1
(a) Total phenolic concentration (TPC) and (b) total flavonoid concentration (TFC) versus rice protein hydrolysate (RPH) concentration. (c) relationship between the TPC and TFC of RPH.
Figure 2
Figure 2
Influence of RPH concentration on the scavenging activity of 1,1-diphenyl-2-picrylhydrazyl (DPPH).
Figure 3
Figure 3
Influence of RPH concentration on the scavenging ability of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS).
Figure 4
Figure 4
Influence of the concentration of RPH on reduction capacity.
Figure 5
Figure 5
Fluorescence decay kinetic curve of the oxygen radical absorbance capacity assay for various samples.
Figure 6
Figure 6
Effect of RPH concentration on hyaluronidase inhibitory activity. The means not sharing a common superscript are significantly different (p < 0.05).
Figure 7
Figure 7
Effect of RPH concentration on tyrosinase-inhibitory activity. Means not sharing a common superscript are significantly different (p < 0.05).
Figure 8
Figure 8
Molecular weight (MW) determination for RPHs through sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE): (a) tricine-SDS-PAGE patterns of the MW marker (line 1) and RPHs (line 2) and (b) the relative content (%) of each MW of RPHs.
Figure 9
Figure 9
MTT assay for the cell toxicity of raw 264.7 cells treated with different RPH concentrations for 24 and 48 h.
See this image and copyright information in PMC

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