Surface Properties of Whey Protein Concentrate Fibrils Selectively Modified by Trypsin
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Abstract:
To gain insight into the effect of proteolysis on the fibril formation and surface properties of whey protein concentrate (WPC), it was selectively modified using trypsin at low degrees of hydrolysis (DH) (0.2%, 0.6%, and 1%) before adjusting the pH to 2.0 and heating at 90 ℃. The microscopic morphology of the aggregates was analyzed using transmission electron microscopy (TEM), and surface properties of the aggregates were also evaluated. The results showed that the fibrils exhibited lower emulsifying activity index (EAI) and emulsifying stability index (ESA), but higher foaming and foam stability than amorphous polymers under similar pH conditions. Trypsin modification was found to promote WPC fibril formation. The EAI was slightly increased compared to native WPC, while foaming and foam stability were significantly increased. The greatest increase in foaming (11.76%) was observed at a DH of 0.6%. At a DH of 1%, the foam stability was increased by 12.59%. Thus, trypsin modification of WPC improved fibril structure and increased surface hydrophobicity of the formed fibril, thus improving the interface properties.
