Structural and Functional Characterization of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance.

ABSTRACT: Amylases are probably the best studied glycoside hydrolases and have a huge biotechnological value for industrial processes on starch. Multiple amylases from fungi and microbes are currently in use. Whereas bacterial amylases are well suited for many industrial processes due to their high stability, fungal amylases are recognized as safe and are preferred in the food industry, although they lack the pH tolerance and stability of their bacterial counterparts. Here, we describe three amylases, two of which have a broad pH spectrum extending to pH 8 and higher stability well suited for a broad set of industrial applications. These enzymes have the characteristic GH13 α-amylase fold with a central (β/α)8-domain, an insertion domain with the canonical calcium binding site and a C-terminal β-san

SUBMITTER: Roth C 

PROVIDER: S-EPMC6801514 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature