Cloning, overexpression, and structural characterization of a novel archaeal thermostable neopullulanase from DSM 2162.

The main purpose of the present study is to introduce the biochemical characteristics of the industrial valuable thermostable pullulan degrading enzyme from DSM2162. Recombinant protein was purified by a combination of thermal treatment and affinity chromatography, with a yield of 15.94% and 7.