Dissolution Behavior of Soy Proteins and Effect of Initial Concentration

The solution concentration profiles of soy protein and its components, glycinin and β-conglycinin, as a function of pH and initial concentration have been measured. The concentration profiles generally followed a U-shaped trend with pH, with a minimum at around pH 4−5. Dissolution concentration unex...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 2007-03, Vol.55 (6), p.2467-2473
Main Authors: Lui, Dora Y. M, White, Edward T, Litster, James D
Format: Article
Language:English
Subjects:
Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts
Antigens, Plant
beta-conglycinin
Biological and medical sciences
chemical concentration
Chemical Precipitation
dissolution
Food industries
food processing
Fundamental and applied biological sciences. Psychology
Globulins - analysis
glycinin
Hydrogen-Ion Concentration
Molecular Structure
protein separation
Seed Storage Proteins
separation
Solubility
Solutions
soy protein
Soybean Proteins - analysis
Soybean Proteins - chemistry
Soybean Proteins - isolation & purification
water solubility
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Summary:The solution concentration profiles of soy protein and its components, glycinin and β-conglycinin, as a function of pH and initial concentration have been measured. The concentration profiles generally followed a U-shaped trend with pH, with a minimum at around pH 4−5. Dissolution concentration unexpectedly increased with the initial concentration of the solution, with the increase being approximately proportional to the increase in initial concentration. The reasons for this are not clear. For the initial concentrations studied, β-conglycinin is undersaturated between pH 5 and 7 and remains in solution, while glycinin becomes supersaturated in the same pH range and precipitates. Therefore separation of the two proteins can be achieved. Keywords: Soy protein solubility; soy flour; protein precipitation; protein separation; glycinin; β-conglycinin.
ISSN:0021-8561
1520-5118
DOI:10.1021/jf062436p