title: Functional analysis of the carbohydrate-binding module of an esterase from Neisseria sicca SB involved in the degradation of cellulose acetate.
abstract: An esterase gene from Neisseria sicca SB encoding CaeA, which catalyzes the deacetylation of cellulose acetate, was cloned. CaeA contained a putative catalytic domain of carbohydrate esterase family 1 and a carbohydrate-binding module (CBM) family 2. We constructed two derivatives, with and without the CBM of CaeA. Binding assay indicated that the CBM of CaeA had an affinity for cellulose.
authors.affiliation: Environmental Technology Research Division, Osaka Municipal Technical Research Institute, Osaka, Japan. moriyosi@omtri.or.jp
authors.forename: Kunihiko
authors.initials: K
authors.lastname: Moriyoshi
authors.forename: Daisuke
authors.initials: D
authors.lastname: Koma
authors.forename: Hayato
authors.initials: H
authors.lastname: Yamanaka
authors.forename: Takashi
authors.initials: T
authors.lastname: Ohmoto
authors.forename: Kiyofumi
authors.initials: K
authors.lastname: Sakai
mesh_terms: D000107:Acetylation; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D001672:Biocompatible Materials; D020134:Catalytic Domain; D002482:Cellulose / Q000031:analogs & derivatives* / Q000378:metabolism; D003001:Cloning, Molecular; D004950:Esterases / Q000235:genetics / Q000378:metabolism*; D042808:Neisseria sicca / Q000201:enzymology*; D011485:Protein Binding
chemical_list: D001426:Bacterial Proteins; D001672:Biocompatible Materials; C005062:acetylcellulose; D002482:Cellulose; D004950:Esterases