Journal
FOOD CHEMISTRY
Volume 141, Issue 2, Pages 992-999Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2013.04.054
Keywords
Mungbean meal; Antioxidant peptides; Virgibacillus sp.; Hydrolyzate; Proteinase
Funding
- Royal Golden Jubilee Ph.D. Program [PhD/0002/2549]
- National Science and Technology Development Agency (NSTDA), Thailand [BT-B-01-FT-19-5014]
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Antioxidant peptides of mungbean meal hydrolysed by Virgibacillus sp. SK37 proteinases (VH), Alcalase (AH) and Neutrase (NH) were investigated. The antioxidant activities based on 2,2'-azinobis (3-ethyl-benzothiazoline-6-sulphonate) (ABTS) radical-scavenging, ferric-reducing antioxidant power (FRAP) and metal chelation of VH were comparable to those of NH. VH was purified using ultrafiltration, ion exchange and gel filtration chromatography. The purified peptides (F37) from VH, which had the highest specific antioxidant activity, consisted of four peptides containing an arginine residue at their C-termini. In addition, the ABTS radical-scavenging activity of the purified peptides (F42) at 0.148 mg/ml was comparable to that of 1 mM of butylated hydroxytoluene (BHT). These two fractions were stable over a wide pH (4-10) and temperature (25-121 degrees C) range. Virgibacillus sp. SK37 proteinase is a potential processing-aid for the production of a mungbean meal hydrolyzate with antioxidant properties. (C) 2013 Elsevier Ltd. All rights reserved.
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