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Literature summary for 3.4.23.1 extracted from
- Myoglobin species with enhanced prooxidative activity is formed during mild proteolysis by pepsin (2004), J. Agric. Food Chem., 52, 1675-1681.
Application
| Application | Comment | Organism |
|---|---|---|
| food industry | treatment with pepsin at pH 4.0 results in lowering the (pseudo)peroxidase activity of metmyoglobin both at physiological pH and at meat pH, leading to strongly enhanced prooxidative effect of mildly proteolyzed metmyoglobin on lipid oxidation | Sus scrofa |
| nutrition | treatment with pepsin at pH 4.0 results in lowering the (pseudo)peroxidase activity of metmyoglobin both at physiological pH and at meat pH, leading to strongly enhanced prooxidative effect of mildly proteolyzed metmyoglobin on lipid oxidation | Sus scrofa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sus scrofa | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| stomach | - |
Sus scrofa | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| metmyoglobin + H2O | - |
Sus scrofa | ? | treatment with pepsin at pH 4.0 results in lowering the (pseudo)peroxidase activity of metmyoglobin both at physiological pH and at meat pH, leading to strongly enhanced prooxidative effect of mildly proteolyzed metmyoglobin on lipid oxidation | ? |  |
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Release 2023.1 (January 2023)
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