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Literature summary for 3.5.3.1 extracted from
- Direct production of L-ornithine from casein by commercial digestive enzymes and in situ activated arginase (2010), Bioprocess Biosyst. Eng., 33, 773-777.
Application
| Application | Comment | Organism |
|---|---|---|
| food industry | when milk casein is hydrolyzed at 37°C by using commercial digestive enzymes, pancreatin F and protease A, a significant accumulation of L-ornithine in the hydrolysate and the simultaneous disappearance of L-arginine is noted. Transient but distinct arginase activity, which is sufficiently high for L-ornithine production, is detected in the hydrolysate for a certain period during casein hydrolysis. Findings suggest that an inactive precursor of arginase is contaminated in pancreatin F and is proteolytically activated during the incubation | Sus scrofa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sus scrofa | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Sus scrofa | - |
| pancreas | - |
Sus scrofa | - |
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Release 2023.1 (January 2023)
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