Comment on “Aggregation Interface and Rigid Spots Sustain the Stable Framework of a Thermophilic N‑Demethylase”
The thermal properties of proteins are very important in industrial, agricultural, and food chemistry. A recent article ( Li, B. , et al. J. Agric. Food Chem. 2023, 71, 5614−5629 ) examines the thermal denaturation of enzymes TrSOX and BSOX by measuring the enthalpy change and melting temperature in...
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| Published in: | Journal of agricultural and food chemistry Vol. 71; no. 49; pp. 19900 - 19902 |
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| Main Authors: | , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
United States
American Chemical Society
13-12-2023
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| Online Access: | Get full text |
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| Summary: | The thermal properties of proteins are very important in industrial, agricultural, and food chemistry. A recent article ( Li, B. , et al. J. Agric. Food Chem. 2023, 71, 5614−5629 ) examines the thermal denaturation of enzymes TrSOX and BSOX by measuring the enthalpy change and melting temperature in the denaturation. In this work, we report the numerical values of entropy in the denaturation of proteins and show that both proteins TrSOX and BSOX exhibit enthalpy–entropy compensation in thermal denaturation, which results in a limited variation of melting temperature in both proteins. Our analysis may serve to improve our understanding of thermal properties in proteins in food chemistry. |
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| Bibliography: | SourceType-Other Sources-1 content type line 63 ObjectType-Correction/Retraction-1 |
| ISSN: | 0021-8561 1520-5118 |
| DOI: | 10.1021/acs.jafc.3c07043 |