Improving the thermostability of the neutral protease of Bacillus stearothermophilus by replacing a buried asparagine by leucine

FEBS Letters

Venema, Gerard²  van der Zee, Rob²  van den Burg, Bertus²  Vriend, Gerrit¹  Eijsink, Vincent G.H.² 

[1] EMBL, Biocomputing Program, Meyerhofstrasse 1, 6900 Heidelberg, Germany;Department of Molecular Genetics, Centre of Biological Sciences, Kerklaan 30, 9751 NN Haren, The Netherlands

关键词: Thermostability;    Neutral protease;    Buried asparagine;    Bacillus stearothermophilus;   

DOI  :  10.1016/0014-5793(91)80434-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Amino acids buried in the hydrophobic interior of a protein with polar side chain atoms, which are not involved in hydrogen bonding or electrostatic interactions, have an adverse effect on protein stability. Replacing such residues by hydrophobic ones may render a protein more stable. Asparagine 241, which is buried in the neutral protease of Bacillus stearothermophilus, was replaced by leucine by side-directed mutagenesis. This mutation increased the stability of the protein by 0.7 ± 0.1 degree.

【 授权许可】

Unknown