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Improvement on the thermal stability and activity of plant cytosolic ascorbate peroxidase 1 by tailing hyper-acidic fusion partners
- Zhang, Mengru, Gong, Ming, Yang, Yumei, Li, Xujuan, Wang, Haibo, Zou, Zhurong
- Biotechnology letters 2015 v.37 no.4 pp. 891-898
- Arabidopsis, Jatropha curcas, ascorbate peroxidase, heat inactivation, heat tolerance, reactive oxygen species, thermal stability
- Cytosolic ascorbate peroxidase 1 (APX1) plays a crucial role in regulating the level of plant cellular reactive oxygen species and its thermolability is proposed to cause plant heat-susceptibility. Herein, several hyper-acidic fusion partners, such as the C-terminal peptide tails, were evaluated for their effects on the thermal stability and activity of APX1 from Jatropha curcas and Arabidopsis. The hyper-acidic fusion partners efficiently improved the thermostability and prevented thermal inactivation of APX1 in both plant species with an elevated heat tolerance of at least 2 °C. These hyper-acidified thermostable APX1 fusion variants are of considerable biotechnological potential and can provide a new route to enhance the heat tolerance of plant species especially of inherent thermo-sensitivity.