Ece, Selin and Evran, Serap and Janda, Jan-Oliver and Merkl, Rainer and , Reinhard (2015) Improving thermal and detergent stability of Bacillus stearothermophilus neopullulanase by rational enzyme design. PROTEIN ENGINEERING DESIGN & SELECTION, 28 (6). pp. 147-151. ISSN 1741-0126, 1741-0134
Full text not available from this repository. (Request a copy)Abstract
Neopullulanase, a glycosyl hydrolase from Bacillus stearothermophilus (bsNpl), is a potentially valuable enzyme for starch and detergent industries. However, as the protein is not active at elevated temperatures and high surfactant concentrations, we aimed to increase its stability by rational enzyme design. Nine potentially destabilizing cavities were identified in the crystal structure of the enzyme. Based on computational predictions, these cavities were filled by residues with bulkier side chains. The five Asp46Glu, Val239Leu, Val404Leu, Ser407Thr and Ala566Leu exchanges resulted in a drastic stabilization of bsNpl against inactivation by heat and detergents. The catalytic activity of the variants was identical to the wild-type enzyme.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SITE-DIRECTED MUTAGENESIS; PROTEIN STABILITY; PULLULANASE; MUTATIONS; THERMOSTABILITY; EXPRESSION; RESIDUES; SUBTILIS; XYLANASE; BINDING; enzyme design; neopullulanase; surfactant stability; thermal stability |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Rainer Merkl |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 11 Jul 2019 13:10 |
| Last Modified: | 11 Jul 2019 13:10 |
| URI: | https://pred.uni-regensburg.de/id/eprint/5378 |
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