Salt-tolerant and thermostable mechanisms of an endoglucanase from marine Aspergillus niger

Abstract The cellulase cocktail of marine Aspergillus niger exhibited salt-tolerant and thermostable properties, which is great potential in industrial application. In order to excavate the single tolerant components from complex cocktail, constitutive homologous expression was employed for direct obtainment endoglucanase ( An EGL). Enzymatic property study revealed that EGL a salt tolerance strong thermostability high salinity environment. Significantly, its activity increased 129% half-life at 65 °C 27.7-fold with presence 4.5 M NaCl. Molecular dynamics simulation Na + Cl ? could form bridges charged residues, then influenced loops stability substrate binding pocket, accounted thermostability. Further, site-specific mutagenesis proved residues Asp95 Asp99 pocket were concern properties. value lignocellulosic utilization conjectural mechanisms referential significance other enzymes. Graphical