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The thermostability of C10 is enhanced by addition of Ca2+ and CR.

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posted on 17.03.2016 by 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

Thermotolerance of the C10 chimera and parental enzymes in the absence of Ca2+ (A), presence of Ca2+ (B), presence of CR (C), and presence of both Ca2+ 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 Ca2+ 0.05 mM or/and CR 6.25×10−3 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.

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