Literature summary for 3.5.1.87 extracted from
Yen, M.; Hsu, W.; Lin, S.
Synthesis of L-homophenylalanine with immobilized enzymes (2010), Process Biochem., 45, 667-674.
No PubMed abstract available
Application
Application |
Comment |
Organism |
synthesis |
a bi-enzyme process for the synthesis of L-homophenylalanine from N-carbamoyl-D-homophenylalanine with immobilized N-acylamino acid racemase and immobilized L-N-carbamoylase. In batch operation, quantitative conversion is achieved. It is a promising alternative for the synthesis of L-homophenylalanine from racemate of N-carbamoyl-DL-homophenylalanine |
Geobacillus kaustophilus |
Cloned(Commentary)
Cloned (Comment) |
Organism |
expressed in Escherichia coli |
Geobacillus kaustophilus |
General Stability
General Stability |
Organism |
the hydrolysis acitvity of the immobilized L-N-carbamoylase drops by 40% after 14 cycles |
Geobacillus kaustophilus |
Inhibitors
Inhibitors |
Comment |
Organism |
Structure |
additional information |
no substrate inhibition is observed |
Geobacillus kaustophilus |
|
Molecular Weight [Da]
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
44000 |
- |
SDS-PAGE |
Geobacillus kaustophilus |
Organism
Organism |
UniProt |
Comment |
Textmining |
Geobacillus kaustophilus |
- |
- |
- |
Purification (Commentary)
Purification (Comment) |
Organism |
purity of 95%, purified enzyme is used for analytical analysis and enzyme immobilization |
Geobacillus kaustophilus |
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
2.91 |
- |
pH 8.0, 50°C, immobilized enzyme |
Geobacillus kaustophilus |
10 |
- |
pH 8.0, 50°C, free enzyme |
Geobacillus kaustophilus |
Substrates and Products (Substrate)
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
additional information |
the enzyme in this study is strigently L-specific |
Geobacillus kaustophilus |
? |
- |
? |
|
Synonyms
Synonyms |
Comment |
Organism |
immobilized L-N-carbamoylase |
- |
Geobacillus kaustophilus |
L-N-carbamoylase |
- |
Geobacillus kaustophilus |
N-carbamoyl-L-amino acid amidohydrolase |
immobilized on Eupergit C |
Geobacillus kaustophilus |
Temperature Optimum [°C]
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
40 |
- |
free enzyme |
Geobacillus kaustophilus |
40 |
50 |
immobilized enzyme |
Geobacillus kaustophilus |
50 |
- |
assay at |
Geobacillus kaustophilus |
Temperature Range [°C]
Temperature Minimum [°C] |
Temperature Maximum [°C] |
Comment |
Organism |
40 |
80 |
upon immobilization the operational pH range and temperature range are markedly broadened, ca. 85% relative activity at 40°C for immoblized enzyme, 100% for free enzyme. At 80°C ca. 35% relative activity for free enzyme and 40% for the immobilized enzyme is observed |
Geobacillus kaustophilus |
Temperature Stability [°C]
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
60 |
- |
the thermostability is significantly enhanced upon immobilization. The free enzyme experiences a decline in activity when the incubation temperature is increased from 50 to 60°C, the activity remains essentially unchanged for the immobilized enzyme. Even at higher temperatures the immobilized enzyme still displays higher thermostabilities than the free enzyme. Incubation at 80°C results in a complete loss of both, the free and immobilized enzyme |
Geobacillus kaustophilus |
80 |
- |
incubation at 80°C results in a complete loss of both, the free and immobilized enzyme |
Geobacillus kaustophilus |
pH Optimum
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
8 |
- |
free and immobilized enzyme |
Geobacillus kaustophilus |
pH Range
pH Minimum |
pH Maximum |
Comment |
Organism |
5 |
11 |
upon immobilization the operational pH range and temperature range are markedly broadened, ca. 35% relative activity at pH 5 for immoblized enzyme, 85% for free enzyme. At pH 11 ca. 60% relative activity for free enzyme and 50% for the immobilized enzyme is observed |
Geobacillus kaustophilus |
pH Stability
pH Stability |
pH Stability Maximum |
Comment |
Organism |
additional information |
- |
the immobilized enzyme exhibits higher pH stability than the free enzyme |
Geobacillus kaustophilus |