Modifying the Physicochemical and Functional Properties of Water-soluble Protein from Mussels by High-pressure Homogenization Treatment

2020 ◽  
Vol 16 (3) ◽  
Author(s):  
Henan Zou ◽  
Ning Zhao ◽  
Xiaojie Shi ◽  
Shuang Sun ◽  
Cuiping Yu
Keyword(s):  
High Pressure ◽  
Functional Properties ◽  
Soluble Protein ◽  
Protein Solubility ◽  
Water Soluble ◽  
Initial Structure ◽  
High Pressure Homogenization ◽  
Homogenization Treatment ◽  
Water Soluble Protein ◽  
Physicochemical And Functional Properties

AbstractThis study investigated the changes in physicochemical and functional properties of water-soluble protein from mussels (MWP) induced by high-pressure homogenization (HPH). The results indicated that HPH treatment unfolded or disrupted the initial structure of MWP, exposing free sulfhydryl groups and buried hydrophobic groups. As the homogenization pressure increased, the aggregation of MWP particles gradually decreased. Moreover, protein solubility and dispersion stability increased in aqueous solution. Foaming and emulsifying properties were also improved. HPH treatment has proven to be an effective technique for enhancing the functional properties of shellfish protein, and 120 MPa was the optimum homogenization pressure to modify MWP.

THE SOLUBLE PROTEINS OF THE MUSCLE TISSUE OF THE HADDOCK

1931 ◽  
Vol 6 (1) ◽  
pp. 1-11 ◽  
Author(s):  
J. F. LOGAN
Keyword(s):  
Sodium Chloride ◽  
Aqueous Solutions ◽  
Muscle Tissue ◽  
Soluble Protein ◽  
Potassium Phosphate ◽  
Extraction Methods ◽  
Water Soluble ◽  
Tabular Form ◽  
Water Soluble Protein ◽  
Isoelectric Points

As a contribution to the chemistry of muscle tissue, the solubility of the protein of haddock muscle in aqueous solutions of sodium chloride and neutral potassium phosphate, respectively, was determined. The results are expressed in tabular form and graphically in the form of solubility curves. A water-soluble protein and also a salt-soluble protein were isolated from dialyzed haddock muscle by extraction methods. These proteins were obtained in a comparatively pure condition by precipitation from solution in the region of their isoelectric points.

High-pressure homogenization influences the functional properties of protein from oyster (Crassostrea gigas)

LWT ◽  
2021 ◽  
pp. 112107
Author(s):  
Zhaofang Liu ◽  
Zixuan Guo ◽  
Di Wu ◽  
Xu Fei ◽  
Hesham R. Ei-Seedi ◽  
...  
Keyword(s):  
High Pressure ◽  
Functional Properties ◽  
Crassostrea Gigas ◽  
High Pressure Homogenization

FRACTIONATION OF LIVETIN AND THE MOLECULAR WEIGHTS OF THE α- AND β-COMPONENTS

1957 ◽  
Vol 35 (4) ◽  
pp. 241-250 ◽  
Author(s):  
W. G. Martin ◽  
J. E. Vandegaer ◽  
W. H. Cook
Keyword(s):  
Light Scattering ◽  
Soluble Protein ◽  
Soluble Fraction ◽  
Egg Yolk ◽  
Water Soluble ◽  
Water Soluble Fraction ◽  
Molecular Weights ◽  
Water Soluble Protein ◽  
Hen Egg Yolk ◽  
Hen Egg

Livetin, the major water-soluble protein of hen egg yolk, was found to contain three major components having mobilities of −6.3, −3.8, and −2.1 cm.2 sec.−1 volt−1 at pH 8, µ 0.1, and these have been designated α-, β-, and γ-livetin respectively. The α- and β-livetins were separated and purified electrophoretically after removal of γ-livetin by precipitation from 37% saturated ammonium sulphate or 20% isopropanol. The α-, β-, and mixed livetins resembled pseudoglobulins in solubility but γ-livetin was unstable and this loss of solubility has, so far, prevented its characterization. Molecular weights determined by light scattering, osmotic pressure, and Archibald sedimentation procedure yielded respectively: 8.7, 7.8, and 6.7 × 104 for α-livetin, and 4.8, 5.0, and4.5 × 104 for β-livetin. Under suitable conditions of sedimentation and electrophoresis, egg yolk has been shown to contain three components having the same behavior as the three livetins of the water-soluble fraction.

Effect of Ginkgo Protein on Moisture Content and Hardness of Bread

2012 ◽  
Vol 531 ◽  
pp. 395-398
Author(s):  
Xiao Fei Sun ◽  
Yu Hui Qiao
Keyword(s):  
Moisture Content ◽  
Shelf Life ◽  
Total Protein ◽  
Soluble Protein ◽  
Water Soluble ◽  
Experimental Results ◽  
Water Soluble Protein

Ginkgo seeds were selected and used as experimental material to study protein compositions in ginkgo protein. Ginkgo protein was used as accessory to be added into flour to make bread. Effect of ginkgo protein on moisture content and hardness of bread were investigated. Experimental results showed that ginkgo protein contained water-soluble protein and salt-soluble protein which was 85.28 percents in total protein and contained small amounts of prolamin and alkali-soluble protein. The bread added with different ratios of ginkgo protein had higher moisture content and lower hardness. Therefore, adding appropriate amount of ginkgo protein could improve bread baking performances and bread shelf life.

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