Why is one Bacillus alpha-amylase more resistant against irreversible thermoinactivation than another?
Open Access
- 1 March 1988
- journal article
- research article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 263 (7), 3092-3096
- https://doi.org/10.1016/s0021-9258(18)69039-8
Abstract
No abstract availableThis publication has 35 references indexed in Scilit:
- Protein engineering of subtilisin BPN': enhanced stabilization through the introduction of two cysteines to form a disulfide bondBiochemistry, 1987
- Why does ribonuclease irreversibly inactivate at high temperatures?Biochemistry, 1986
- Cumulative effect of intragenic amino-acid replacements on the thermostability of a proteinNature, 1986
- Cloning in Bacillus subtilis of an extremely thermostable alpha amylase: Comparison with other cloned heatstable alpha amylasesBiochemical and Biophysical Research Communications, 1984
- On the role of reversible denaturation (unfolding) in the irreversible thermal inactivation of enzymesBiotechnology & Bioengineering, 1983
- Rapid measurement of free amino acids in serum and CSF using high-performance liquid chromatographyLife Sciences, 1981
- PROTEIN THERMOSTABILITY.International Journal of Peptide and Protein Research, 1981
- Purification and Characterization of a Thermostable alpha‐Amylase from Bacillus licheniformisStarch ‐ Stärke, 1979
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- A New, Heat Stable Bacterial Amylase and its Use in High Temperature LiquefactionStarch ‐ Stärke, 1973