Abstract
The peanut proteins were extracted from cold pressed and hot pressed peanut meal in this work. Emulsifying properties of cross-linking between cold pressed peanut/hot pressed peanut and fish (Decapterus maruadsi) protein hydrolysates catalyzed by transglutaminase were investigated. Electrophoresis indicated that cross-linked proteins were formed in all the transglutaminase-treated samples, and the susceptibility of cold pressed peanut or hot pressed peanut subunits to transglutaminase was enhanced by addition of the (Decapterus maruadsi) protein hydrolysates. For the cross-linked cold pressed peanut-(Decapterus maruadsi) protein hydrolysates and hot pressed peanut-(Decapterus maruadsi) protein hydrolysates protein conjugates, the surface area mean diameter d32, volume mean diameter d43, creaming index, and instability decreased after TGase treatment. Besides, the addition of (Decapterus maruadsi) protein hydrolysates could remedy the disadvantage of essential amino acids (e.g., Thr, Met, and Lys) deficiency in cold pressed or hot pressed peanut. For cold pressed peanut or hot pressed peanut, transglutaminase treatment had no effect on the emulsifying activity but the emulsion stability was improved.
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