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Some functional properties of oat bran protein concentrate modified by trypsin

Guan, X., Yao, H., Chen, Z., Shan, L., Zhang, M.
Food chemistry 2007 v.101 no.1 pp. 163-170
protein concentrates, polypeptides, trypsin, foaming capacity, proteolysis, enzymatic hydrolysis, protein hydrolysates, oat bran, water holding capacity, solubility, protein degradation, emulsifying properties, globulins, emulsions, foams
Oat bran protein concentrate (OBPC) was prepared from oat bran, and hydrolyzed using trypsin. Protein hydrolysates of three different degrees of hydrolysis (4.1%, 6.4% and 8.3% respectively) were obtained. SDS-PAGE analysis demonstrated that oat globulin was the major protein component in OBPC. After trypsin treatment, acidic polypeptides were partly degraded into large peptides (Mr = 29,000-33,000) and small peptides (Mr < 20,000); however, basic polypeptides were almost intact. The functional properties of the resulting products were compared with those of control OBPC. Marked changes in the protein functionality were caused by proteolysis. The solubility, water-holding capacity, emulsifying activity and foaming ability of the hydrolysates gradually increased with the increase in DH. However, the oil-holding capacity, emulsifying stability and foaming stability of the hydrolysates reduced to a certain extent.