Abstract
An α-amylase encoding gene from the extremely thermophilic Archaea Thermococcus hydrothermalis was cloned and expressed in Escherichia coli . The encoded α-amylase possesses molecular characteristics specific to the Archaea, especially from Pyrococcus species, with biochemical characteristics of the α-amylases from Thermococcus . The gene is 1374 bp long and encodes a protein of 457 amino acids composed of a 22 amino acid putative signal peptide and a 435 amino acid mature protein (calculated molecular mass 49 236 Da). The T. hydrothermalis recombinant α-amylase is optimally active at 75–85°C and at pH 5.0–5.5.

This publication has 0 references indexed in Scilit: