Keywords
Rice Protein Antioxidant Activity Bioactive Peptide In Vitro Digestion
Abstract
In order to study the antioxidant activity of rice albumin, globulin, gliadin and glutenin in vitro digestion products, Osborne method was used to extract four rice proteins from rice flour. Gastric-trypsin step-by-step enzymatic hydrolysis was used to comprehensively evaluate the antioxidant activity of the digested products using four indicators: DPPH?, ABTS+?, ?OH free radical scavenging ability and Fe2+ metal ion chelating ability. Compared with commercially available soy peptides, four rice proteins have good antioxidant activity after simulated in vitro digestion. Among them, the digestion product of gliadin has the best antioxidant activity. The half-inhibitory concentrations of DPPH?, ABTS+?, ?OH free radical scavenging ability and Fe2+ metal ion chelating ability are 30.88 mg/mL, 27.61 mg/mL, and 5.43 mg respectively. /mL, 0.18 mg/mL. The half-inhibitory concentrations of Fe2+ chelating ability of the four proteolytic products of rice are all less than 1 mg/mL, indicating good Fe2+ chelating ability. The research results show that the in vitro digestion enzymatic hydrolysates of four rice proteins have different sizes of antioxidant activities, with molecular weights concentrated in the range of 181 to 1000 Da. They are antioxidant peptides that are easily absorbed by the human body. The Osborne method consisting of a 2-step in vitro digestion of rice flour was used to extract albumin, globulin, prolamin, and glutelin by using pepsin and trypsin. Subsequently, the antioxidant activity of the resultant rice digest was studied in terms of 2, 2-diphenyl-1-picrylhydrazyl (DPPH?), 2,2¡ä-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS+?) and ?OH radical scavenging as well as Fe2+-chelating activity. The results revealed that the in vitro digests of four rice proteins exhibited better antioxidant activity than commercial soybean peptides. Among these, the digest of prolamin showed the highest antioxidant activity, where the half-maximal inhibitory concentration (IC50) values of DPPH?, ABTS+?, and ?OH radical-scavenging as well as Fe2+-chelating activities were 30.88, 27.61, 5.43, and 0.18 mg/mL, respectively. The enzymatic hydrolysates of albumin, globulin, prolamin, and glutelin showed good Fe2+-chelating activities with IC50 values < 1 mg/ mL. The results indicated that the in vitro digests of the four rice proteins tested in this study showed different antioxidant activities and that the molecular weights of these small peptides were in a range of 181~1000 Da, which is similar to that od antioxidant peptides that can be absorbed easily in humans.
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Original research done by Tong Litao
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