Characterization of Nocardiopsis beta-1,3-glucanase with additional carbohydrate-binding domains.
beta-1,3-Glucanase F (BglF) from alkaliphilic Nocardiopsis sp. F96 is a single domain enzyme composed of only a catalytic domain. Chimeric BglFs with some carbohydrate-binding domains were constructed and characterized. By connecting the C-terminal additional domain of beta-1,3-glucanase H from Bacillus circulans IAM1165 and the chitin-binding domain of chitinase J from alkaliphilic Bacillus sp. J813, binding ability and hydrolyzing activity toward insoluble beta-1,3-glucans were both improved.
Koizumi
Naoya
N
Department of Bioengineering, Tokyo Institute of Technology, Midori-ku, Yokohama 226-8501, Japan.
Isoda
Yuya
Y
Maeda
Kiyoe
K
Masuda
Sumiko
S
Fibriansah
Gunter
G
Kumasaka
Takashi
T
Yatsunami
Rie
R
Fukui
Toshiaki
T
Nakamura
Satoshi
S
D000192:Actinomycetales / Q000201:enzymology*; D001407:Bacillus / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D043326:Glucan 1,3-beta-Glucosidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism
D001426:Bacterial Proteins; D011134:Polysaccharides; D011993:Recombinant Fusion Proteins; D043326:Glucan 1,3-beta-Glucosidase