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The Mechanism of Irreversible Enzyme Inactivation at 100°C
Abstract
The mechanism of irreversible thermoinactivation of an enzyme has been quantitatively elucidated in the pH range relevant to enzymatic catalysis. The processes causing irreversible inactivation of hen egg-white lysozyme at 100°C are deamidation of asparagine residues, hydrolysis of peptide bonds at aspartic acid residues, destruction of disulfide bonds, and formation of incorrect (scrambled) structures; their relative contributions depend on the p H.
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Citations
Cited by
Instability and decay of the primary structure of DNA
Lindahl, T. (1993) · Nature · doi:10.1038/362709a0 · Cited by 5,679
Tertiary Structure Is a Principal Determinant to Protein Deamidation
Kossiakoff, A. A. (1988) · Science · doi:10.1126/science.3353715 · Cited by 186
Reversible and irreversible unfolding of multi-domain proteins
Strucksberg, K. H., Rosenkranz, T., & Fitter, J. (2007) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.09.005 · Cited by 55
Metadata
- Authors
- Ahern, T. J., & Klibanov, A. M.
- Venue
- Science
- Published
- 1985-06-14
- Volume
- 228
- Issue
- 4705
- Pages
- 1280-1284
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2026530009
- Cited by
- 446
- References
- 0
- FWCI
- 6.13
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: The Mechanism of Irreversible Enzyme Inactivation at 100°C. https://app.cochat.ai/papers/10.1126/science.4001942
- The paper
- Ahern, T. J., & Klibanov, A. M. (1985). The Mechanism of Irreversible Enzyme Inactivation at 100°C. Science. https://doi.org/10.1126/science.4001942
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
