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

2Citations
Citations of this article
10Readers
Mendeley users who have this article in their library.

This article is free to access.

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.

Cite

CITATION STYLE

APA

Koizumi, N., Isoda, Y., Maeda, K., Masuda, S., Fibriansah, G., Kumasaka, T., … Nakamura, S. (2007). Characterization of Nocardiopsis beta-1,3-glucanase with additional carbohydrate-binding domains. Nucleic Acids Symposium Series (2004), (51), 459–460. https://doi.org/10.1093/nass/nrm230

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free