4.7 Article

Analysis of texture properties and water-soluble fraction proteome of sea cucumber body wall with different boiling heating treatment

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FOOD CHEMISTRY
卷 409, 期 -, 页码 -

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ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2022.135333

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Sea cucumber; Texture; Label -free quantitative proteomic; Collagen fibres; Fibrillin microfibrils

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Label-free quantitative proteomic analysis was used to identify the key proteins affecting the texture properties of sea cucumber body wall under different boiling heating treatments. The results showed that the abundance of proteins in the water-soluble fraction increased during boiling heating treatment, mainly consisting of structural proteins such as collagens, microfibril-associated proteins, glycoproteins, and muscle proteins. The degradation of these structural proteins was believed to cause the disintegration of collagen fibers and FMs network skeleton as well as gelatinization, leading to a decrease in hardness and shear force. Additionally, the degradation of FMs occurred layer by layer during boiling heating treatment, with fibrilin-1 outer layer degrading first followed by the fibrilin-2 core component.
Label-free quantitative proteomic analysis was utilized to determine the key proteins that affect texture prop-erties of sea cucumber body wall (SCBW) with different boiling heating treatment. 862, 363, 315, and 258 proteins were confirmed in water-soluble fractions from fresh group, 0.5 h-, 2 h-and 4 h-heat treatment group, respectively. During boiling heating treatment, proteins with an increased abundance in water-soluble fraction primarily belong to structural proteins, such as collagens, microfibril-associated proteins, glycoproteins, and muscle proteins. It was speculated that the degradation of these structural proteins caused the progressive disintegration of network skeleton of collagen fibres and FMs as well as the gelatinization, thus resulted in the decrease of hardness and shear force. Besides, the degradation of FMs was occurred layer by layer during boiling heating treatment, and the fibrilin-1 outer layer degraded first, followed by the fibrilin-2 core component.

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