αs1-Casein Film Prepared Using Transglutaminase
- 1 April 1987
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 51 (4), 993-996
- https://doi.org/10.1080/00021369.1987.10868166
Abstract
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 αs1-casein solution with transglutaminase was applied to the preparation of an αs1-casein film. The αs1-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 αs1-casein film as a supporting material of immobilized enzymes, a medical polymer and an edible film.This publication has 8 references indexed in Scilit:
- Gelation mechanism of protein solution by transglutaminase.Agricultural and Biological Chemistry, 1986
- Gelation of Casein and Soybean Globulins by TransglutaminaseAgricultural and Biological Chemistry, 1985
- [46] TransglutaminasesMethods in Enzymology, 1985
- Gelation of casein and soybean globulins by transglutaminase.Agricultural and Biological Chemistry, 1985
- Functional properties of food proteins polymerized by transglutaminase.Agricultural and Biological Chemistry, 1984
- TransglutaminasesAnnual Review of Biochemistry, 1980
- [38] The rapid determination of amino groups with TNBSMethods in Enzymology, 1972
- Purification and Some of the Properties of αs-Casein and κ-CaseinJournal of Dairy Science, 1963