Oxidation of Cathepsin D by Hydroxy Radical: Its Effect on Enzyme Structure and Activity against Myofibrillar Proteins Extracted from <i>Coregonus peled</i>
In this study, cathepsin D was oxidized in vitro with different concentrations of H<sub>2</sub>O<sub>2</sub>, and the activity, structure, and extent of myofibrillar protein degradation by oxidized cathepsin D were evaluated. The sulfhydryl content of cathepsin D decreased to...
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2023-06-01
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author | Mengjie Ma Pingping Liu Chaoye Wang Xiaorong Deng Lianfu Zhang Jian Zhang |
author_facet | Mengjie Ma Pingping Liu Chaoye Wang Xiaorong Deng Lianfu Zhang Jian Zhang |
author_sort | Mengjie Ma |
collection | DOAJ |
description | In this study, cathepsin D was oxidized in vitro with different concentrations of H<sub>2</sub>O<sub>2</sub>, and the activity, structure, and extent of myofibrillar protein degradation by oxidized cathepsin D were evaluated. The sulfhydryl content of cathepsin D decreased to 9.20% after oxidation, while the carbonyl content increased to 100.06%. The β-sheet in the secondary structure altered due to oxidation as well. The changes in the intrinsic fluorescence and UV absorption spectra indicated that oxidation could cause swelling and aggregation of cathepsin D molecules. The structure of cathepsin D could change its activity, and the activity was highest under 1 mM H<sub>2</sub>O<sub>2</sub>. Cathepsin D could degrade myofibrillar proteins in different treatment groups, and the degree of degradation is various. Therefore, this study could provide a scientific basis for the mechanism of interaction among hydroxyl radical oxidation, cathepsin D, and MP degradation. |
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spelling | doaj.art-e246eb225048422ba1b22462c3d9e31d2023-11-18T17:08:27ZengMDPI AGMolecules1420-30492023-06-012813511710.3390/molecules28135117Oxidation of Cathepsin D by Hydroxy Radical: Its Effect on Enzyme Structure and Activity against Myofibrillar Proteins Extracted from <i>Coregonus peled</i>Mengjie Ma0Pingping Liu1Chaoye Wang2Xiaorong Deng3Lianfu Zhang4Jian Zhang5Key Laboratory of Agricultural Product Processing and Quality Control of Specialty (Co-Construction by Ministry and Province), School of Food Science and Technology, Shihezi University, Shihezi 832003, ChinaKey Laboratory of Agricultural Product Processing and Quality Control of Specialty (Co-Construction by Ministry and Province), School of Food Science and Technology, Shihezi University, Shihezi 832003, ChinaKey Laboratory of Agricultural Product Processing and Quality Control of Specialty (Co-Construction by Ministry and Province), School of Food Science and Technology, Shihezi University, Shihezi 832003, ChinaKey Laboratory of Agricultural Product Processing and Quality Control of Specialty (Co-Construction by Ministry and Province), School of Food Science and Technology, Shihezi University, Shihezi 832003, ChinaState Key Laboratory of Food Science and Technology, School of Food Science and Technology, Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Jiangnan University, Wuxi 214122, ChinaKey Laboratory of Agricultural Product Processing and Quality Control of Specialty (Co-Construction by Ministry and Province), School of Food Science and Technology, Shihezi University, Shihezi 832003, ChinaIn this study, cathepsin D was oxidized in vitro with different concentrations of H<sub>2</sub>O<sub>2</sub>, and the activity, structure, and extent of myofibrillar protein degradation by oxidized cathepsin D were evaluated. The sulfhydryl content of cathepsin D decreased to 9.20% after oxidation, while the carbonyl content increased to 100.06%. The β-sheet in the secondary structure altered due to oxidation as well. The changes in the intrinsic fluorescence and UV absorption spectra indicated that oxidation could cause swelling and aggregation of cathepsin D molecules. The structure of cathepsin D could change its activity, and the activity was highest under 1 mM H<sub>2</sub>O<sub>2</sub>. Cathepsin D could degrade myofibrillar proteins in different treatment groups, and the degree of degradation is various. Therefore, this study could provide a scientific basis for the mechanism of interaction among hydroxyl radical oxidation, cathepsin D, and MP degradation.https://www.mdpi.com/1420-3049/28/13/5117cathepsin Dmyofibrillar proteinprotein oxidation<i>Coregonus peled</i> |
spellingShingle | Mengjie Ma Pingping Liu Chaoye Wang Xiaorong Deng Lianfu Zhang Jian Zhang Oxidation of Cathepsin D by Hydroxy Radical: Its Effect on Enzyme Structure and Activity against Myofibrillar Proteins Extracted from <i>Coregonus peled</i> Molecules cathepsin D myofibrillar protein protein oxidation <i>Coregonus peled</i> |
title | Oxidation of Cathepsin D by Hydroxy Radical: Its Effect on Enzyme Structure and Activity against Myofibrillar Proteins Extracted from <i>Coregonus peled</i> |
title_full | Oxidation of Cathepsin D by Hydroxy Radical: Its Effect on Enzyme Structure and Activity against Myofibrillar Proteins Extracted from <i>Coregonus peled</i> |
title_fullStr | Oxidation of Cathepsin D by Hydroxy Radical: Its Effect on Enzyme Structure and Activity against Myofibrillar Proteins Extracted from <i>Coregonus peled</i> |
title_full_unstemmed | Oxidation of Cathepsin D by Hydroxy Radical: Its Effect on Enzyme Structure and Activity against Myofibrillar Proteins Extracted from <i>Coregonus peled</i> |
title_short | Oxidation of Cathepsin D by Hydroxy Radical: Its Effect on Enzyme Structure and Activity against Myofibrillar Proteins Extracted from <i>Coregonus peled</i> |
title_sort | oxidation of cathepsin d by hydroxy radical its effect on enzyme structure and activity against myofibrillar proteins extracted from i coregonus peled i |
topic | cathepsin D myofibrillar protein protein oxidation <i>Coregonus peled</i> |
url | https://www.mdpi.com/1420-3049/28/13/5117 |
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