The thermostability of C10 is enhanced by addition of Ca<sup>2+</sup> and CR.
Chia-Jung Chang
Cheng-Chung Lee
Yueh-Te Chan
Devin L. Trudeau
Mei-Huey Wu
Chih-Hsuan Tsai
Su-May Yu
Tuan-Hua David Ho
Andrew H.-J. Wang
Chwan-Deng Hsiao
Frances H. Arnold
Yu-Chan Chao
10.1371/journal.pone.0147485.g006
https://plos.figshare.com/articles/figure/The_thermostability_of_C10_is_enhanced_by_addition_of_Ca_sup_2_sup_and_CR_/3958302
<p>Thermotolerance of the C10 chimera and parental enzymes in the absence of Ca<sup>2+</sup> (A), presence of Ca<sup>2+</sup> (B), presence of CR (C), and presence of both Ca<sup>2+</sup> and CR (D). Purified cellulases (1μg) were pre-incubated in 50 mM sodium acetate buffer (pH 5.0) at different temperatures for 10 min with or without additional Ca<sup>2+</sup> 0.05 mM or/and CR 6.25×10<sup>−3</sup> mM. The residual enzyme activity was then determined on 1% PASC at pH 5.0 at their optimal temperature for 6 hrs. The 100% value of relative activity refers to the optimal activity of each enzyme without thermal treatment.</p>
2016-03-17 23:57:18
structure-guided SCHEMA recombination
Cellulase Thermostability
SCHEMA calculations
SCHEMA non-contiguous recombination algorithm
enzyme
heat treatment
GsCelA
BsCel 5A Analyzing
PC
chimeric C 10
animal feed industries
Geobacillus bacteria
crystal structure determinations
thermostable chimeric cellulase C 10
BsCel 5A
3 10 helix
thermostability
novel tool
CR
chimeric proteins
mutagenesis analyses
protein sequences
crown ether
mechanism
thermophilic Geobacillus sp
Bacillus homolog
Structure-Guided Recombination Cellulases