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Literature summary for 2.3.2.13 extracted from
- pH-stability and thermal properties of microbial transglutaminase-treated whey protein isolate (2010), J. Agric. Food Chem., 58, 1946-1953.
Application
| Application | Comment | Organism |
|---|---|---|
| nutrition | MTGase treatment significantly increases the denaturation temperature of beta-lactoglobulin in whey protein isolate, from 71.84°C in the untreated sample to 78.50°C after 30 h of incubation with MTGase. Increase in ´denaturation temperature is primarily due to covalent cross-linking and not due to an increase in nonpolar interactions within the protein. The surface hydrophobicity of the protein decreases upon cross-linking, due to occlusion of the hydrophobic cavities to the fluorescent probes. The cross-linked protein exhibits a U-shaped pH-stability profile with maximumturbidity at pH 4.0-4.5 | Streptomyces mobaraensis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces mobaraensis | - |
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