Transglutaminase is a Ca2+-dependent enzyme that covalently polymerizes proteins through the formation of ε-(γ-glutamyl)lysyl cross-links. We have reported that highly concentrated protein solutions were firmly gelatinized by transglutaminase. The technique of gelation of an αsl-casein solution with transglutaminase was applied to the preparation of an αsl-casein film. The αsl-casein film obtained showed a high tensile strength (105 g/cm2) and strain (72%). It was insoluble in water, 10% 2-mercaptoethanol, 6.6 m urea, 10% SDS and 6 m guanidine hydrochloride. Even if it was diluted with water and then heated at 100°C for 10 min, it remained insoluble. However, it was gradually hydrolyzed by chymotrypsin. These results suggest the usefulness of the αsl-casein film as a supporting material of immobilized enzymes, a medical polymer and an edible film. © 1987, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.
CITATION STYLE
Motoki, M., Aso, H., Seguro, K., & Nio, N. (1987). αsl-Casein Film Prepared Using Transglutaminase. Agricultural and Biological Chemistry, 51(4), 993–996. https://doi.org/10.1271/bbb1961.51.993
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