Effect of introducing disulfide bridges in C-terminal structure on the thermostability of xylanase XynZF-2 from Aspergillus niger
Author:
Affiliation:
1. School of Life Science and Technology, Xinxiang Medical University
2. Synthetic Biology Engineering Lab of Henan Province
Publisher
Microbiology Research Foundation
Subject
Applied Microbiology and Biotechnology,Microbiology
Link
https://www.jstage.jst.go.jp/article/jgam/65/5/65_2018.11.002/_pdf
Reference38 articles.
1. Bai, W., Yang, L., and Ma, Y. J. (2014) Improving thermal stability of xylanase by introducing aromatic residues at the N-terminus. Chin. J. Biotechnol., 30, 1217–1224.
2. Bu, Y., Cui, Y., Ying, P., Hu, M., Tian, Y. et al. (2018) Engineering improved thermostability of the GH11 xylanase from neocallimastix patriciarum, via computational library design. Appl. Microbiol. Biot., 102, 1–11.
3. Chang, X., Xu, B., Bai, Y., Luo, H., Ma, R. et al. (2017) Role of N-linked glycosylation in the enzymatic properties of a thermophilic GH 10 xylanase from Aspergillus Fumigatus expressed in pichia pastoris. PLoS One, 12, e0171111.
4. Chen, X. Z., Xu, S. Q., Zhu, M. S., Cui, L. S., Zhu, H. et al. (2010) Site-directed mutagenesis of an Aspergillus niger xylanase B and itsexpression, purification and enzymatic characterization in Pichia pastoris. Process Biochem., 45, 75–80.
5. Chen, Y., Li, T., Li, J., Cheng, S., Wang, J. et al. (2017) Stabilization of peptides against proteolysis through disulfide-bridge conjugation with synthetic aromatics. Org. Biomol. Chem., 15, 1921–1929.
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