Characterization of Nocardiopsis beta-1,3-glucanase with additional carbohydrate-binding domains

Naoya Koizumi; Yuya Isoda; Kiyoe Maeda; Sumiko Masuda; Gunter Fibriansah; Takashi Kumasaka; Rie Yatsunami; Toshiaki Fukui; Satoshi Nakamura

doi:10.1093/nass/nrm230

Characterization of Nocardiopsis beta-1,3-glucanase with additional carbohydrate-binding domains

Nucleic Acids Symp Ser (Oxf). 2007:(51):459-60. doi: 10.1093/nass/nrm230.

Authors

Naoya Koizumi¹, Yuya Isoda, Kiyoe Maeda, Sumiko Masuda, Gunter Fibriansah, Takashi Kumasaka, Rie Yatsunami, Toshiaki Fukui, Satoshi Nakamura

Affiliation

¹ Department of Bioengineering, Tokyo Institute of Technology, Midori-ku, Yokohama 226-8501, Japan.

PMID: 18029785
DOI: 10.1093/nass/nrm230

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Actinomycetales / enzymology*
Bacillus / enzymology
Bacterial Proteins / chemistry*
Bacterial Proteins / genetics
Bacterial Proteins / metabolism
Binding Sites
Glucan 1,3-beta-Glucosidase / chemistry*
Glucan 1,3-beta-Glucosidase / genetics
Glucan 1,3-beta-Glucosidase / metabolism
Polysaccharides / chemistry
Polysaccharides / metabolism*
Protein Structure, Tertiary
Recombinant Fusion Proteins / chemistry
Recombinant Fusion Proteins / metabolism

Substances

Bacterial Proteins
Polysaccharides
Recombinant Fusion Proteins
Glucan 1,3-beta-Glucosidase