A novel approach to the evaluation of hydrophobicity of food proteins

Danilenko, A. N.; Dianova, V. T.; Braudo, E. E.; Henning, T.; Mothes, R.; Schwenke, K. D.

doi:10.1002/(sici)1521-3803(199808)42:03/04<179::aid-food179>3.3.co;2-2

Cited by 7 publications

(5 citation statements)

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“…The differential scanning calorimetry (DSC) method is commonly used to characterize the thermal stability of the proteins. However, since the latter strongly depends on the protein interactions with the surrounding solvent it can be indirectly used to estimate the surface hydrophobicity of the protein [45]. The latter is related to the change in the heat capacity upon denaturation of the protein.…”

Section: Resultsmentioning

confidence: 99%

The Role of Buffers in Wild-Type HEWL Amyloid Fibril Formation Mechanism

Brudar

Hribar-Lee

2019

Biomolecules

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Amyloid fibrils, highly ordered protein aggregates, play an important role in the onset of several neurological disorders. Many studies have assessed amyloid fibril formation under specific solution conditions, but they all lack an important phenomena in biological solutions—buffer specific effects. We have focused on the formation of hen egg-white lysozyme (HEWL) fibrils in aqueous solutions of different buffers in both acidic and basic pH range. By means of UV-Vis spectroscopy, fluorescence measurements and CD spectroscopy, we have managed to show that fibrillization of HEWL is affected by buffer identity (glycine, TRIS, phosphate, KCl-HCl, cacodylate, HEPES, acetate), solution pH, sample incubation (agitated vs. static) and added excipients (NaCl and PEG). HEWL only forms amyloid fibrils at pH = 2.0 under agitated conditions in glycine and KCl-HCl buffers of high enough ionic strength. Phosphate buffer on the other hand stabilizes the HEWL molecules. Similar stabilization effect was achieved by addition of PEG12000 molecules to the solution.

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Section: Resultsmentioning

confidence: 99%

The Role of Buffers in Wild-Type HEWL Amyloid Fibril Formation Mechanism

Brudar

Hribar-Lee

2019

Biomolecules

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“…electrostatic interactions which may occur between the dye and the protein need to be taken in consideration when interpreting the results. Compared to other methods like theoretical calculations based on the amino acid sequence, chromatography ( 117 ), differential scanning calorimetry, or precision densimetry ( 118 ), the use of fluorescent dyes is relatively rapid and simple and can also be applied to proteins with unknown amino acid sequences. Cardamone and Puri established a method to quantitatively assess the relative surface hydrophobicity by calculating the association constant of ANS-protein binding from Klotz plots ( 119 ) and compared the results with RP-HPLC and a theoretical hydrophobicity index based on the amino acid sequence ( 30 ).…”

Section: Applications Of Fluorescent Dyes In Protein Characterizationmentioning

confidence: 99%

Extrinsic Fluorescent Dyes as Tools for Protein Characterization

2008

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Abstract. Noncovalent, extrinsic fluorescent dyes are applied in various fields of protein analysis, e.g. to characterize folding intermediates, measure surface hydrophobicity, and detect aggregation or fibrillation. The main underlying mechanisms, which explain the fluorescence properties of many extrinsic dyes, are solvent relaxation processes and (twisted) intramolecular charge transfer reactions, which are affected by the environment and by interactions of the dyes with proteins. In recent time, the use of extrinsic fluorescent dyes such as ANS, Bis-ANS, Nile Red, Thioflavin T and others has increased, because of their versatility, sensitivity and suitability for high-throughput screening. The intention of this review is to give an overview of available extrinsic dyes, explain their spectral properties, and show illustrative examples of their various applications in protein characterization.

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“…In the course of legumin limited trypsinolysis C-terminal parts of a-chains are split off [13]. The stable product of limited trypsinolysis of legumin -legumin-T, with molecular mass 240 kDa [14] is characterized by higher surface hydrophobicity [15] and improved emulsion activity [16] in comparison to legumin.…”

Section: Complexes Of Faba Bean Legumin and Legumin-t With Chitosanmentioning

confidence: 99%

Plant protein interactions with polysaccharides and their influence on legume protein functionality A Review

Braudo

Плащина

Schwenke³

2001

Nahrung

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Associative interactions between proteins and polysaccharides, both coulombic and non-coulombic, lead to the formation of interpolymer complexes. Complex formation with charged polysaccharides, either anionic or cationic, imparts solubility to seed globulins in the vicinity of their isoelectric points. This has been shown for the complexes "sunflower 11 S globulin (helianthinin)--sodium alginate" and "faba bean legumin (or the product of its limited proteolysis with trypsin--legumin-T)--chitosan". Hysteresis effects allow to control the solubility of seed globulins in weakly acid or weakly basic media. Formation of soluble complexes of faba bean legumin or legumin-T with chitosan substantially increases the emulsion stability of the both proteins.

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A novel approach to the evaluation of hydrophobicity of food proteins

Cited by 7 publications

References 0 publications

The Role of Buffers in Wild-Type HEWL Amyloid Fibril Formation Mechanism

The Role of Buffers in Wild-Type HEWL Amyloid Fibril Formation Mechanism

Extrinsic Fluorescent Dyes as Tools for Protein Characterization

Plant protein interactions with polysaccharides and their influence on legume protein functionality A Review

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