Functional analysis of the carbohydrate-binding module of an esterase from Neisseria sicca SB involved in the degradation of cellulose acetate.
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.
Moriyoshi
Kunihiko
K
Environmental Technology Research Division, Osaka Municipal Technical Research Institute, Osaka, Japan. moriyosi@omtri.or.jp
Koma
Daisuke
D
Yamanaka
Hayato
H
Ohmoto
Takashi
T
Sakai
Kiyofumi
K
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
D001426:Bacterial Proteins; D001672:Biocompatible Materials; C005062:acetylcellulose; D002482:Cellulose; D004950:Esterases