Back to Search
Start Over
Thermostabilization of Bacillus amyloliquefaciens α-amylase by chemical cross-linking
- Source :
-
Journal of Biotechnology . Jun2006, Vol. 123 Issue 4, p434-442. 9p. - Publication Year :
- 2006
-
Abstract
- Abstract: Chemical cross-linking of a mesophilic α-amylase from Bacillus amyloliquefaciens (BAA) was carried out. Intra-molecular cross-links between lysine residues upon treatment of the enzyme with ethylene glycol bis(succinic acid N-hydroxy succinimide ester) resulted in enhancement of thermostability as indicated by irreversible thermoinactivation experiments. Enhancement of thermostability coincided with a dramatic protection against aggregation, combined with a decrease in surface hydrophobicity. Deamidation, another important mechanism of irreversible thermoinactivation, was also diminished upon modification. While no significant changes in the kinetic parameters are evident, rigidification of the protein structure is suggested by circular dichroism (CD) and fluorescence studies. [Copyright &y& Elsevier]
- Subjects :
- *ETHYLENE glycol
*AMINO acids
*ORGANIC compounds
*LYSINE
Subjects
Details
- Language :
- English
- ISSN :
- 01681656
- Volume :
- 123
- Issue :
- 4
- Database :
- Academic Search Index
- Journal :
- Journal of Biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 20869137
- Full Text :
- https://doi.org/10.1016/j.jbiotec.2005.12.017