17E-24 |
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P. GICHUHI, Dept. of Food & Nutritional Sciences, Tuskegee Univ., College of Agricultural, Environmental & Natural Sciences, Tuskegee, AL 36088 and Y.-H. P. Hsieh, Dept. of Nutrition, Food & Exercise Sciences, Florida State Univ., 436 Sandels Bldg., Tallahassee, FL 32306-1493. Cannonball jellyfish (Stomolophus meleagris) is one of the edible species common in the coastal waters of the United States where it is underutilized. Edible jellyfish (JF) are mainly consumed by people from eastern Asia, where processed jellyfish is a multi-million dollar industry in some countries. Consumption of JF has traditionally been linked with therapeutic effects such as alleviation of arthritis among other diseases. Previous JF collagen studies related the collagen to different types (I, II, III, IV, and V). The objectives of this study were to quantify and partially characterize the collagen from the cannonball JF. To extract the collagen, the JF tissues were first minced, homogenized and lyophilized. The lyophilized tissues were subsequently extracted with water, alkaline, acid and the collagen solubilized with pepsin. The pepsin-solubilized extracts were salt precipitated and the fractions analyzed by SDS-PAGE. The major precipitate fractions were characterized by CM-cellulose chromatography, CNBr peptide mapping and Micro-DSC III. The pepsin-solubilized extracts were the major fractions for both the legs and the umbrella, 55% and 45%, respectively. Salt precipitation of the pepsin-solubilized fraction revealed the 3.0 M and 3.5 M NaCl precipitates as the major constituent at neutral pH. Electrophoretic patterns of all the salt-precipitated fractions were very similar to each other and to that of vertebrate type II collagen standard. However, the CM-cellulose chromatography and CNBr analyses of the 3.0 M and 3.5 M NaCl precipitate displayed a possibility of more than one type of a-chain. The DSC thermograms of the 3.0 M and 3.5 M NaCl precipitate had one main transition like that of type II collagen. The cannonball JF collagen closely resembled type II collagen standard than the other collagen types, although the possibility of multiple a-chains indicates otherwise.
Session 17E, Food Chemistry: Proteins
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