Production and purification of antioxidant peptides from a mungbean meal hydrolysate by Virgibacillus sp SK37 proteinase

被引:61
作者
Lapsongphon, Nawaporn [1 ]
Yongsawatdigul, Jirawat [1 ]
机构
[1] Suranaree Univ Technol, Sch Food Technol, Food Prot Res Unit, Nakhon Ratchasima 30000, Thailand
关键词
Mungbean meal; Antioxidant peptides; Virgibacillus sp; Hydrolyzate; Proteinase; RADIATA L. WILCZEK; IDENTIFICATION; DIGESTS;
D O I
10.1016/j.foodchem.2013.04.054
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
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.
引用
收藏
页码:992 / 999
页数:8
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