Thermostable chitinase from Caldicellulosiruptor saccharolyticus strain EP2: Cloning, expression, and biochemical characterization

Chitin waste, a byproduct of chitin-rich material processing, poses significant environmental challenges, emphasizing the need for efficient waste management and bioconversion strategies. While chitinase enzymes have been extensively studied, the identification of thermostable chitinases with a unique mode of action remains critical for advancing chitin degradation and producing high-value products. In this study, the recombinant chitinase ChiA1 from Caldicellulosiruptor saccharolyticus strain EP2 was characterized for its thermostability and enzymatic activity. ChiA1 exhibited an optimal temperature of 70°C and retained considerable activity even at 90°C, demonstrating excellent thermostability. The enzyme also showed an optimal pH of 6.0 and was capable of degrading both colloidal chitin and chitin extracted from shrimp shells. Hydrolysis profiling revealed that ChiA1 cleaved chitin chains through an endo-mode of action, breaking internal glycosidic bonds within the polymer structure. The exceptional thermostability and catalytic properties of ChiA1 suggest its potential for applications in industrial processes that require high-temperature conditions, such as bioconversion of chitin waste into valuable bio-products. Overall, this study provides novel insights into the functionalities of ChiA1, offering promising prospects for its use in future biotechnological applications related to chitin degradation and utilization.