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KMID : 1007519950040030194
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Food Science and Biotechnology
1995 Volume.4 No. 3 p.194 ~ p.199
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Heat-Induced and Transglutaminase-Catalyzed Gelations of Coconut Proteins
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Kwon, KiSung
Bae, DongHo/Rhee, Khee Choon
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Abstract
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Both heat-induced and transglutaminase-catalyzed gelations of the coconut albumin and globulin fractions, and total protein were studied to obtain information on their gelling properties for their possible application in gel-based foods.
The rate of beat-induced gelation was affected by temperature. While less than 20% of the globulin fraction was aggregated even after an extended heating time at 100℃, over 45% of the albumins and the total protein were aggregated at 90℃ for 10 min. SDS-PAGE of gels showed that when the temperature is increased, the soluble aggregates break down to form insoluble aggregates of high molecular weights. Overall the rate of thermal gelation increased in the presence of dithiothreitol, and it decreased when N-ethylmaleimide was added. Also, heating caused a decrease in the amount of sulfhydryl (SH) groups in the precipitate of the protein samples, indicating that the free SH groups are involved in the formation of protein gel structure. In transglutaminase-catalyzed gelation. SDS-PAGE indicated that coconut proteins were polymerized by the microbial transglutaminase. It was confirmed that the gel from 2% coconut total protein solution was formed by transglutaminase-catalyzed polymerization. These results may indicate feasibility of their application to protein gel-based foods.
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