4.7 Article

Modification of functional, rheological and structural characteristics of myofibrillar proteins by high-intensity ultrasonic and papain treatment

Journal

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.ifset.2021.102748

Keywords

Enzyme; Emulsification; Foaming properties; Sonication; Solubility

Funding

  1. Deakin University through the Alfred Deakin research fellowship

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In this study, the effects of sonication duration and papain enzyme treatment on myofibrillar proteins were investigated. It was found that longer sonication time and enzyme treatment contributed to improvements in water holding capacity, solubility, foaming, and emulsifying properties, while also causing changes in the proteins' secondary structure. Additionally, the combination of papain treatment and shorter sonication time resulted in the highest values for surface hydrophobicity, specific surface area, net charge, storage modulus, solubility, and water holding capacity. Conversely, longer sonication time showed reductions in solubility, water holding capacity, and surface hydrophobicity, as well as increases in particle size distribution and protein turbidity.
The effects of sonication duration (15 and 30 min) and papain enzyme treatments on the conformational, physicochemical and functional traits of myofibrillar proteins (MPs) were addressed in this study. As the ultrasound duration was increased, the water holding capacity (WHC), solubility, foaming and emulsifying properties were improved as a result of the changes in the particles size distribution and zeta potential. Our results indicated that the turbulence force caused increments in the surface hydrophobicity and significant changes in the secondary structure. Also, the rheological properties were influenced by both cavitation force and papain treatment. According to the observations, the samples treated with sonication (for 15 and 30 min) and enzyme were more elastic with higher viscosity, as compared to the control. Compared with the control, enzymolyzed samples indicated better functionality. Moreover, papain treatment led to the increase of the hydrophobicity groups on the surface of proteins and the decrease of the amount of alpha-helix and beta-sheet structures. It was noteworthy that the most changes in the structure and techno-functionality of myofibrillar proteins were observed for the sample affected by the simultaneous application of papain treatment and 15 min sonication. The highest values in the surface hydrophobicity, specific surface area, net charge, storage modulus, solubility and WHC belonged to this sample. However, enzyme-modified samples exposed to the longer sonication time (30 min) demonstrated reductions in solubility, WHC and surface hydrophobicity, as well as increases in the particle size distribution and protein turbidity.

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