Protein–Phenolic Interactions as a Factor Affecting the Physicochemical Properties of White Bean Proteins
Abstract
:1. Introduction
2. Results
2.1. UV-Vis Spectra of Protein–Phenolic Complexes
2.2. Changes in Content of Free Amino Groups, Thiol Groups, and Tryptophan Residues of Proteins Affected by Phenolic Compounds
2.3. Size-Exclusion High-Performance Liquid Chromatography (SE-HPLC)
2.4. Polyacrylamide Gel Electrophoresis
2.5. Effect of pH and Ionic Strength on the Solubility of Protein–Phenolic Complexes
2.6. FT-IR Spectral Analysis
2.7. Binding Capacity of Proteins for Phenolic Compounds and Stability of Complexes
3. Discussion
3.1. UV-Vis Spectra of Protein–Phenolic Complexes
3.2. Changes in the Content of Proteins, Free Amino Groups, Thiol Groups, and Tryptophan Residues Affected by Phenolic Compounds
3.3. Size-Exclusion High-Performance Liquid Chromatography
3.4. Polyacrylamide Gel Electrophoresis
3.5. Effect of pH and Ionic Strength on the Solubility of Protein–Phenolics Complexes
3.6. FT-IR Spectral Analysis
3.7. Binding Capacity of Protein for Phenolic Compounds and Stability of Complexes
4. Materials and Methods
4.1. Chemicals
4.2. Plant Materials
4.3. Extraction of Protein Fractions
4.3.1. Isolation of Albumins
4.3.2. Isolation of Globulins
4.4. Extraction of Phenolic Compounds from Plant Materials
4.5. Incubation of Proteins with Phenolic Compounds
4.6. UV-Vis Spectra of Protein–Phenolic Complexes
4.7. Changes in Content of Proteins Free Amino Groups, Thiol Groups, and Tryptophan Residues Affected by Phenolic Compounds
4.7.1. Effect of Phenolic Compounds on The Content of Free Amino Groups
4.7.2. Effect of Phenolic Compounds on the Content of Free Thiol Groups
4.7.3. Effect of Phenolic Compounds on the Free Tryptophan Residues
4.8. Size-Exclusion High-Performance Liquid Chromatography
4.9. Polyacrylamide Gel Electrophoresis
4.9.1. SDS-PAGE
4.9.2. Native-PAGE
4.10. Effect of pH and Ionic Strength on The Solubility of Protein–Phenolics Complexes
4.10.1. Effect of pH
4.10.2. Effect of Ionic Strength
4.11. FT-IR Spectral Analysis
4.12. Binding Capacity of Protein for Phenolic Compounds and Stability of Complexes
4.12.1. Binding Capacity of Protein for Phenolic Compounds
4.12.2. Effect of pH on the Desorption Stability of Protein–Phenolic Complexes
4.12.3. Effect of Ionic Strength on the Desorption Stability of Protein–Phenolic Complexes
4.13. Determination of Phenolic Contents by HPLC
4.14. Statistical Analysis
5. Conclusions
Supplementary Materials
Author Contributions
Funding
Conflicts of Interest
References
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Sample Availability: Samples of the compounds are not available from the authors. |
Sample | Albumins | Globulins | ||
---|---|---|---|---|
Phenolics Bound µmol/g Protein ± SD | ||||
Phenolics | GA | 172.2 Aa ± 5.32 | 157.4 Bc ± 4.02 | |
FA | 5.5 Ac ± 2.15 | 6.2 Ae ± 2.32 | ||
CGA | 174.6 Ba ± 5.12 | 187.5 Aa ± 6.50 | ||
Q | 149.4 Ab ± 6.95 | 131.4 Bc ± 7.72 | ||
A | 8.9 Ac ± 2.24 | 7.1 Ad ± 2.22 | ||
CAT | 157.3 Ab ± 6.84 | 165.3 Ab ± 6.12 | ||
Extracts | GT | GCAT | 5.2 Bf ± 0.82 | 11.3 Ad ± 0.61 |
EGCAT | 21.0 Ac ± 1.09 | 19.3 Ac ± 1.39 | ||
CAT | 174.3 Ba ± 2.25 | 184.6 Aa ± 4.37 | ||
ECAT | 8.6 Be ± 0.23 | 10.0 Ae ± 0.65 | ||
EGCATG | 89.3 Ab ± 1.09 | 86.2 Ab ± 2.97 | ||
ECATG | 12.1 Ad ± 0.54 | 8.5 Bf ± 0.63 | ||
GC | NCGA | 7.1 Bd ± 0.33 | 11.7 Ac ± 0.55 | |
CGA | 212.9 Ba ± 8.12 | 231.5 Aa ± 7.11 | ||
CCGA | 10.9 Bb ± 1.18 | 18.5 Ab ± 2.72 | ||
FQA | 10.8 Bb ± 0.42 | 3.3 Af ± 0.43 | ||
3,4-DCQA | 2.9 B ± 0.30 | 3.8 Aef ± 0.59 | ||
3,5-DCQA | 8.9 Ac ± 0.61 | 9.7 Ad ± 1.71 | ||
4,5-DCQA | 3.9 Be ± 0.48 | 4.1 Ae ± 0.33 |
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Sęczyk, Ł.; Świeca, M.; Kapusta, I.; Gawlik-Dziki, U. Protein–Phenolic Interactions as a Factor Affecting the Physicochemical Properties of White Bean Proteins. Molecules 2019, 24, 408. https://doi.org/10.3390/molecules24030408
Sęczyk Ł, Świeca M, Kapusta I, Gawlik-Dziki U. Protein–Phenolic Interactions as a Factor Affecting the Physicochemical Properties of White Bean Proteins. Molecules. 2019; 24(3):408. https://doi.org/10.3390/molecules24030408
Chicago/Turabian StyleSęczyk, Łukasz, Michał Świeca, Ireneusz Kapusta, and Urszula Gawlik-Dziki. 2019. "Protein–Phenolic Interactions as a Factor Affecting the Physicochemical Properties of White Bean Proteins" Molecules 24, no. 3: 408. https://doi.org/10.3390/molecules24030408