Improvement of shark type I collagen with microbial transglutaminase in urea.
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.
Nomura
Y
Y
Applied Protein Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Fuchu, Japan. ny318@cc.tuat.ac.jp
Toki
S
S
Ishii
Y
Y
Shirai
K
K
D000818:Animals; D003094:Collagen / Q000737:chemistry*; D004548:Elasticity; D012754:Sharks / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology; D011503:Transglutaminases / Q000737:chemistry*; D014508:Urea / Q000737:chemistry*; D014783:Viscosity
D014508:Urea; D003094:Collagen; D011503:Transglutaminases