Antioxidative properties of partially purified barley hordein, rice bran protein fractions and their hydrolysates

• Published in: Journal of cereal science Vol. 49; no. 3; pp. 422 - 428
• Main Authors: Chanput, Wasaporn, Theerakulkait, Chockchai, Nakai, Shuryo
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 01.05.2009; Elsevier
• Subjects: albumins; antioxidant activity; antioxidants; Antioxidative properties; barley; Barley hordein; Biological and medical sciences; Cereal and baking product industries; Food industries; Fundamental and applied biological sciences. Psychology; globulins; glutelins; hordein; Hydrolysates; linoleic acid; lipid peroxidation; prolamins; protein hydrolysates; purification; rice bran; Rice bran protein; Rice bran protein; Antioxidative properties; Barley hordein; Hydrolysates; Hordein; Barley; Hydrolysate; Cereal; Antioxidant; Protein; Rice bran
• ISSN: 0733-5210; 1095-9963
• DOI: 10.1016/j.jcs.2009.02.001

Antioxidative properties of proteins from barley and rice bran and their hydrolysates were examined. Three major hordein fractions of barley, B, C and D hordeins, were partially purified by gel filtration. Albumin, globulin, prolamin and glutelin fractions of rice bran were fractioned by the Osborne method. Hydrolysates of these protein fractions were prepared by digesting with pepsin followed by trypsin. Antioxidant properties in terms of antioxidative activity against linoleic acid peroxidation and reducing activity without the lipid adjuvant were investigated. The globulin fraction from rice bran protein revealed the strongest antioxidative activity throughout the incubation time of 7 days ( p ≤ 0.05). The albumin fraction of rice bran protein showed the highest reducing activity (6964 μmol of Fe 2+) followed by globulin, prolamin, glutelin and hordein fractions with activities of 2904, 2017, 1809 and 1333 μmol of Fe 2+, respectively ( p ≤ 0.05). Partially purified C hordein exhibited the highest reducing activity compared with B and D hordeins. Protein hydrolysates obtained after digestion with pepsin and trypsin exhibited much greater antioxidative, as well as reducing, activities than those from before digestion.