Abstract
In the presence of urea, type I collagen could form a gel with crosslinks with microbial transglutaminase (MTGase). Collagen self-assembly was accelerated with the addition of MTGase. The proportion of reconstructed collagen fibrils was raised with the addition of MTGase. MTGase-treated collagen gel remained gelled at high temperatures at which collagen denatured. By treatment with MTGase, collagen could form the gel under impossible condition to collagen self-assembly, and that denaturation temperature was raised.
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Nomura, Y., Toki, S., Ishii, Y., & Shirai, K. (2001). Improvement of shark type I collagen with microbial transglutaminase in urea. Bioscience, Biotechnology and Biochemistry, 65(4), 982–985. https://doi.org/10.1271/bbb.65.982
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