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