[Review: Prize-awarded article] Structural and Functional Study of Novel Carbohydrate-Active enZymes

Author:

Fushinobu Shinya1

Affiliation:

1. Department of Biotechnology, The University of Tokyo

Publisher

The Japanese Society of Applied Glycoscience

Subject

General Medicine

Reference53 articles.

1. 2) B.L. Cantarel, P.M. Coutinho, C. Rancurel, T. Bernard, V. Lombard and B. Henrissat: The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res., 37, D233-238 (2009).

2. 7) X. Liu, Y. Qu, F. You and Y. Liu: Studies on the key amino acid residues responsible for the alkali-tolerance of the xylanase by site-directed or random mutagenesis. J. Mol. Cat. B, 18, 307-313 (2002).

3. 9) F. de Lemos Esteves, V. Ruelle, J. Lamotte-Brasseur, B. Quinting and J.M. Frere: Acidophilic adaptation of family 11 endo-β-1,4-xylanases: modeling and mutational analysis. Protein Sci., 13, 1209-1218 (2004).

4. 10) B. Al Balaa, K. Brijs, K. Gebruers, J. Vandenhaute, J. Wouters and I. Housen: Xylanase XYL1p from Scytalidium acidophilum: site-directed mutagenesis and acidophilic adaptation. Bioresour. Technol., 100, 6465-6471 (2009).

5. 11) T. Sakata, H. Miyakubo, Y. Osada, R. Wada, H. Takahashi, R. Yatsunami, T. Fukui and S. Nakamura: Functional improvement of xylanase by intoducing mutated xylan-binding domain. J. Appl. Glycosci., 53, 131-136 (2006).

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