Substrate Specificities of GH8, GH39, and GH52 β-xylosidases from Bacillus halodurans C-125 Toward Substituted Xylooligosaccharides
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Applied Microbiology and Biotechnology,Biochemistry,General Medicine,Bioengineering,Biotechnology
Link
http://link.springer.com/content/pdf/10.1007/s12010-020-03451-2.pdf
Reference43 articles.
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4. Kaneko, S., Kuno, A., Fujimoto, Z., Shimizu, D., Machida, S., Sato, Y., Yura, K., Go, M., Mizuno, H., Taira, K., Kusakabe, I., & Hayashi, K. (1999). An investigation of the nature and function of module 10 in a family F/10 xylanase FXYN of Streptomyces olivaceoviridis E-86 by module shuffling with the Cex of Cellulomonas fimi and site-directed mutagenesis. FEBS Letters, 460(1), 61–66.
5. Kaneko, S., Iwamatsu, S., Kuno, A., Fujimoto, Z., Sato, Y., Yura, K., Go, M., Mizuno, H., Taira, K., Hasegawa, T., Kusakabe, I., & Hayashi, K. (2000). Module shuffling of a family F/10 xylanase: Replacement of modules M4 and M5 of the FXYN of Streptomyces olivaceoviridis E-86 with those of the Cex of Cellulomonas fimi. Protein Engineering, Design & Selection, 13(12), 873–879.
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