期刊
FOOD HYDROCOLLOIDS
卷 47, 期 -, 页码 51-60出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2015.01.007
关键词
Structure-function relationship; Peanut protein; Peanut oil emulsion; Enzymatic demulsification; Aqueous extraction
资金
- National Natural Science Foundation of China [31171652]
- Program for Science & Technology Innovation Talents in Universities of Henan Province [13HASTIT005]
We isolated and characterized various proteins (adsorbed and unadsorbed) from the aqueous extract emulsion of peanut seeds. The peanut emulsion was further subjected to a freeze-thaw treatment or enzymatic hydrolysis by the alkaline endopeptidase Mifong(R)2709. The proteins in the residual cream layer and the aqueous phase, obtained from the freeze-thaw treatment as well as the cream layer peptides and aqueous phase peptides obtained at various periods of hydrolysis (namely 5, 10, 30, and 60 min), were isolated and analyzed for structural (molecular weight, disulfide bond content, and surface hydrophobicity) and surface (dynamic interfacial tension, emulsifying activity, and stability indices) properties. The peanut proteins adsorbed at the oil-water interface showed superior emulsification properties and unique structural characteristics consisting of large molecular weight proteins and small molecular weight oleosins, and also possessed a higher disulfide bond content and greater surface hydrophobicity. The proteins in the residual cream layer derived from the freeze-thaw treatment had a higher disulfide bond content, surface hydrophobicity, and emulsification indices than the proteins in the aqueous phase. In contrast, following the hydrolysis of the emulsion, the resulting cream layer peptides and the aqueous phase peptides exhibited a significantly lower disulfide bond content, weaker surface hydrophobicity and lower emulsification indices than the intact proteins. These protein structural changes following hydrolysis contributed to the destabilization of the peanut emulsions. We also observed a positive correlation for the disulfide bond content and the surface hydrophobicity with the emulsifying activity index (EAI), R-2 = 0.963 and 0.982, respectively as well as the emulsion stability index (ESI), R-2 = 0.920 and 0.906, respectively. (C) 2015 Elsevier Ltd. All rights reserved.
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