Isolation, Purification, and Biochemical Characterization of a Novel Water Soluble Protein from Inca Peanut (PlukenetiavolubilisL.)

2002 ◽  
Vol 50 (17) ◽  
pp. 4906-4908 ◽  
Author(s):  
Shridhar K. Sathe ◽  
Bruce R. Hamaker ◽  
Kar Wai Clara Sze-Tao ◽  
Mahesh Venkatachalam
Keyword(s):  
Soluble Protein ◽  
Biochemical Characterization ◽  
Water Soluble ◽  
Water Soluble Protein

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.

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.

scholarly journals Studies on silk proteins I. The properties and constitution of fibroin. The conversion of fibroin into a water-soluble form and its bearing on the phenomenon of denaturation

1947 ◽  
Vol 190 (1021) ◽  
pp. 145-169 ◽  
Keyword(s):  
Molecular Weight ◽  
Soluble Protein ◽  
Optical Rotation ◽  
Amino Nitrogen ◽  
Water Soluble ◽  
Soluble Form ◽  
Secondary Process ◽  
Amide Nitrogen ◽  
Water Soluble Protein ◽  
The Mean

Some of the constituent amino-acids of fibroin (degummed silk) are determined. Special attention is directed to histidine, owing to its use in the calculation of the molecular weight of fibroin. A value of 0⋅45% has been found by methods in which the histidine is isolated as nitranilate or di-(3:4-dichlorobenzenesulphonate). Other values obtained are serine 12⋅6%, threonine 1⋅5%, tyrosine 10⋅6%, and proline 1⋅5%. Hydroxyproline appears to be absent, but the presence of small amounts of some hydroxyamino-acid other than serine and threonine is indicated. The mean residue weight of fibroin is determined by three methods, one of which is a new method based on analysis of the complex formed between fibroin and cupri-ethylenediamine. This method gives a Cu:fibroin-N ratio of 1:1⋅92 and, if allowance is made for co-ordination with the tyrosine hydroxy1 group, an equivalence of 1⋅964 atoms of peptide-nitrogen to 1 atom of copper is obtained. The three methods give an average value of 78⋅0 for the mean residue weight of fibroin. This value, together with the most acceptable data for amino-acid constituents, indicate that the unidentified anhydro-residues (about 20%) have a mean residue weight of about 107. Evidence is presented that fibroin contains no amide-nitrogen. Methods for the determination of amide-nitrogen at present in use, which indicate a content of 1 to 2%, are considered to be unreliable. Fibroin dissolved in cupri-ethylenediamine gives, on neutralization and dialysis of the resulting solution, a water-soluble protein. The production of this water-soluble protein is attended by little or no degradation of the original fibroin as shown by determinations of fluidity, amino-nitrogen, and acid- and alkali-combining power. The water-soluble protein is precipitated by the normal protein-precipitating reagents, but in every instance examined the precipitated material exhibits an insolubility comparable with that of the original fibroin. Factors responsible for the solubilization process are investigated and data for molecular weight, titration values, ultra-violet absorption spectra, reducing activity, optical rotation, tryptic hydrolysis, and viscosity for both soluble and dispersed fibroin are given. Soluble fibroin has [ α ] D 15 — 53⋅1° and dispersed fibroin [ α ] D 15 — 58⋅9°, both in aqueous media. The preparation and properties of films and filaments of fibroin are described. Films of fibroin can be prepared that are water-soluble. On stretching, these films show strain-birefringence, acquire considerable tensile strength, and become insoluble in water, but X-ray examination gives the β -keratin pattern for both the stretched and unstretched films. Reasons are advanced for considering the water-soluble form of fibroin to be the native or renatured protein and the original protein to be the denatured form. The denaturation of fibroin is discussed on the basis that denaturation is essentially an unfolding of a coiled long-chain molecule. The subsequent aggregation of the uncoiled molecules to give an insoluble product is considered to be a secondary process. Some aspects of protein and polypeptide chains as macro-molecules are also discussed.

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