摘要：Abstract pH and pKa’s are important parameters in enzyme technology, because they determine the protonated states of titratable groups and thus influence the structure, dynamics, and functions of proteins. Specifically, experimental studies of Thermomyces lanuginosus SSBP revealed the presence of putative family 18 chitinases are triggered by low pHs. In this work, we performed several pH-based molecular dynamics simulations of chitinase II in a water solvent. This work was aimed at establishing the optimum activity and stability profiles of chitinase II. We observed a strong conformational pH dependence of chitinase II and the enzyme retained their characteristic TIM barrel topology at low pH.
