Premium
pH Dependence of Complex Formation Between Condensed Tannins and Proteins
Author(s) -
OH HOONIL,
HOFF JOHAN E.
Publication year - 1987
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1987.tb14059.x
Subject(s) - isoelectric point , chemistry , salt (chemistry) , tannin , ionic strength , chromatography , ultrafiltration (renal) , turbidity , inorganic chemistry , biochemistry , food science , aqueous solution , organic chemistry , oceanography , enzyme , geology
The interaction between condensed grape tannins and some proteins was studied turbidimetrically. Tannins precipitated protein efficiently at pH values up to the isoelectric point of the individual protein. At slightly higher pH values there was a sharp decrease in complex formation. This “critical pH” was usually observed within approximately 0.5 pH unit of the isoelectric point. A close correlation (r = 0.96) was obtained between the isoelectric point and the critical pH of proteins. The effects of pH and ionic strength on turbidity formation by tannins and bovine serum albumin showed that an increasing salt concentration tended to increase turbidity at pH 3, but it had no significant effect at pH 4. In contrast at pH 5 high salt concentration tended to decrease turbidity. Employing an ultrafiltration technique, the binding behavior of interacting tannin and protein was described by a typical Brunauer type II adsorption curve.