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Glucan‐Protein Interactions. Gelatin‐Induced Solubilization of Glycogen in Alcohol‐Water Solutions
Author(s) -
Doyle R. J.,
Woodside E. E.
Publication year - 1971
Publication title -
starch ‐ stärke
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.62
H-Index - 82
eISSN - 1521-379X
pISSN - 0038-9056
DOI - 10.1002/star.19710230205
Subject(s) - gelatin , chemistry , glycogen , solubility , polysaccharide , methanol , solvent , ethanol , fractionation , glucan , butanol , solubilization , organic chemistry , chromatography , phenol , biochemistry
In organic solvents, gelatin can induce the solubilization of glycogen and other polysaccharides. It was shown that the solubilization reaction was mediated through polysaccharide‐protein hydrogen bonds. Glycogen‐gelatin binding was influenced by the relative concentration of glycogen to the protein. The induced solubilization of glycogen was partially inhibited by temperatures above 0 °C. Water was shown to inhibit glycogen‐gelatin interactions in acidified methanol, ethanol, n‐propanol and tertiary butanol. In general, it was found that the most hydrophobic alcohols were the best solvents for the glycogen‐gelatin solubilization reaction. The solubility of the glycogen‐gelatin complex was determined and found to be 0.22 mg/ml. The presence of strong acids tended to inhibit complex formation while weak acids promoted the solubilization reaction. A method for the fractionation of gelatin into distinct molecular weight classes was developed by use of a methanol‐phenol solvent system. High molecular weight gelatins were better glycogen solubilizing agents than low molecular weight gelatins.