Increasing the thermal stability of euphauserase. A cold-active and multifunctional serine protease from Antarctic krill.

摘要: A molecular model of Antarctic krill euphauserase based on the known crystal structure its fiddler crab analog, collagenase I, indicates that core these enzymes is almost identical. Euphauserase a cold-active and thermally sensitive enzyme with high affinity for Lys, Arg large hydrophobic amino acids. Residue Phe137 in euphauserase, localized loop D (autolysis loop), highly exposed surface molecule. Therefore, it appeared to be an easy target autolysis. The broadly specific has low negatively charged residues. In order increase stability enzyme, two mutants were created which residue was replaced by Glu Asp residue. Both mutations resulted increased recombinant towards thermal inactivation.