title: Immobilization of alkaline phosphatase on magnetic particles by site-specific and covalent cross-linking catalyzed by microbial transglutaminase.
abstract: Bacterial alkaline phosphatase (BAP) was site-specifically and covalently immobilized on magnetic particles (MPs) using the enzymatic reaction of microbial transglutaminase (MTG). Immobilization efficiency was affected by the chemical surface treatment of MPs and immobilized BAP exhibited more than 90% of the initial activity after 10 rounds of recycling.
authors.affiliation: Department of Applied Chemistry, Graduate School of Engineering, Kyushu University, 744 Motooka, Fukuoka 819-0395, Japan.
authors.forename: Kousuke
authors.initials: K
authors.lastname: Moriyama
authors.forename: Kyunga
authors.initials: K
authors.lastname: Sung
authors.forename: Masahiro
authors.initials: M
authors.lastname: Goto
authors.forename: Noriho
authors.initials: N
authors.lastname: Kamiya
mesh_terms: D000469:Alkaline Phosphatase / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry; D002384:Catalysis; D004800:Enzymes, Immobilized / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology; D008280:Magnetics; D013379:Substrate Specificity; D011503:Transglutaminases / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D004800:Enzymes, Immobilized; D011503:Transglutaminases; D000469:Alkaline Phosphatase