Folding thermodynamics of PET-hydrolyzing enzyme Cut190 depending on Ca2+ concentration

• Published in: Journal of thermal analysis and calorimetry Vol. 135; no. 5; pp. 2655 - 2663
• Main Authors: Inaba, Satomi, Kamiya, Narutoshi, Bekker, Gert-Jan, Kawai, Fusako, Oda, Masayuki
• Format: Journal Article
• Language: English
• Published: Cham Springer International Publishing 01.03.2019; Springer Nature B.V
• Subjects: Analytical Chemistry; Binding; Calcium ions; Chemistry; Chemistry and Materials Science; Crystal structure; Denaturation; Dichroism; Dynamic structural analysis; Enthalpy; Enzymes; Folding; Glass transition temperature; Inorganic Chemistry; Measurement Science and Instrumentation; Molecular dynamics; Physical Chemistry; Polyethylene terephthalate; Polymer Sciences; Stability analysis; Structural analysis; Temperature; Thermal stability; Thermodynamics; Variations; Molecular dynamics simulations; DSC; Protein conformational change; Circular dichroism

The enzyme, cutinase from Saccharomonospora viridis AHK190 (Cut190), can hydrolyze the inner block of polyethylene terephthalate (PET). Cut190 has a unique feature that both its activity and thermal stability are increased upon Ca 2+ binding. In consideration of the glass transition temperature of P...