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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