title: Improvement of shark type I collagen with microbial transglutaminase in urea.
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.
authors.affiliation: Applied Protein Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Fuchu, Japan. ny318@cc.tuat.ac.jp
authors.forename: Y
authors.initials: Y
authors.lastname: Nomura
authors.forename: S
authors.initials: S
authors.lastname: Toki
authors.forename: Y
authors.initials: Y
authors.lastname: Ishii
authors.forename: K
authors.initials: K
authors.lastname: Shirai
mesh_terms: 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
chemical_list: D014508:Urea; D003094:Collagen; D011503:Transglutaminases