Co-Authors:
Shomer, I., Institute for Technology and Storage of Agricultural Products, Agricultural Research Organization, The Volcani Center, P.O. Bos 6, Bet Dagan 50250, Israel
Vasiliver, R., Institute for Technology and Storage of Agricultural Products, Agricultural Research Organization, The Volcani Center, P.O. Bos 6, Bet Dagan 50250, Israel
Salomon, R., Institute of Piant Protection, Agricultural Research Organization, The Volcani Center, P.O. Bos 6, Bet Dagan 50250, Israel
Abstract:
The structure of coagulated proteins of a serum of citrus fruit aqueous peel extract (SPEX) was studied, considering protein interactions with colloidal cloud constituents. The coagulates’ structural properties are affected by the coagulation conditions such as enzymatic pectin degradation (EPD), temperature, pH, concentration, and tissue origin (flavedo or albedo). The electrophoretic profiles were characteristic for each coagulation temperature but were not affected by the concentration level. The ultrastructure was highly dependent on the coagulating conditions, and different samples appeared in various patterns such as fibrils, spongelike structures, granules, amorphous patterns, and aggregates. Without EPD, the coagulation was suppressed in the SPEX, while it appeared, but delicately, in the flavedo extract. Following the EPD treatment, distinct coagulates were obtained, which appeared as aggregated granules. © 1991, American Chemical Society. All rights reserved.
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