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Ultrasound treatment improved the physicochemical characteristics of cod protein and enhanced the stability of oil-in-water emulsion

Ma, Wuchao, Wang, Jiamei, Xu, Xianbing, Qin, Lei, Wu, Chao, Du, Ming
Food research international 2019 v.121 pp. 247-256
actin, adsorption, disulfide bonds, droplets, emulsions, hydrophobicity, microstructure, moieties, myosin light chains, oils, particle size, polyacrylamide gel electrophoresis, tropomyosins, ultrasonic treatment, ultrasonics
Effects of ultrasonic pretreatment on the physicochemical changes of cod protein and the characteristics of subsequent oil-in-water emulsions were investigated. Ultrasonic treatment led to a reduction of particle size of cod protein. With increasing ultrasonic power, a significant increase in surface hydrophobicity of cod protein was found, due to the decrease of aggregates size as well as protein conformational changes of protein, but a decrease in total sulfhydryl group content was observed, probably because of the formation of disulfide bonds. Ultrasonic pretreatment promoted the adsorption of cod protein on oil droplets, resulting in higher ratios of adsorbed proteins. Diagonal electrophoresis illustrated that larger aggregates in adsorbed proteins were composed of cod actin. Reducing SDS-PAGE showed that adsorbed proteins contained a large amount of cod actin and two faint bands of light chains of myosin, and non-adsorbed proteins were composed of actin, tropomyosin, and the three light chains of myosin. More homogenous microstructures with smaller size of oil droplets were observed for the emulsions stabilized by higher intensity ultrasound treated cod protein, and the coalescence effect was improved obviously. The enhancement of the stability of cod protein coated-oil emulsions might be due to the smaller size of oil droplets and reduced oil droplets attraction by higher ratios of adsorbed proteins.