Probing the role of asparagine mutation in thermostability of Bacillus KR-8104 α-amylase
Authors:
- Mahsa RahimzadehMRMahsa Rahimzadeh
- Khosro KhajehKKKhosro Khajeh
- Manoochehr MirshahiMMManoochehr Mirshahi
- Mahmood KhayatianMKMahmood Khayatian
- Robert SchwarzenbacherRSRobert Schwarzenbacher
- 1 May 2012
- journal article
- research article
- Published by Elsevier in International Journal of Biological Macromolecules
- Vol. 50 (4) , 1175-1182
Abstract
No abstract availableKeywords
Funding Information
- Universität Salzburg
- Tarbiat Modares University
This publication has 43 references indexed in Scilit:
- Thermodynamics and mechanism of protonated asparagine decompositionJournal of the American Society for Mass Spectrometry, 2009
- Enhancing thermostability of maltogenic amylase from Bacillus thermoalkalophilus ET2 by DNA shufflingThe FEBS Journal, 2006
- Structure‐dependent nonenzymatic deamidation of glutaminyl and asparaginyl pentapeptidesChemical Biology & Drug Design, 2004
- Developments in industrially important thermostable enzymes: a reviewBioresource Technology, 2003
- Microbial α-amylases: a biotechnological perspectiveProcess Biochemistry, 2003
- Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for ThermostabilityMicrobiology and Molecular Biology Reviews, 2001
- Protein engineering of bacterial α-amylasesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
- Probing structural determinants specifying high thermostability in Bacillus licheniformis α-amylase 1 1Edited by A. R. FershtJournal of Molecular Biology, 2000
- Stabilization of Enzymes against Thermal Inactivation1983
- Protein Denaturation1968