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Literature summary for 3.4.17.B1 extracted from

  • Sommaruga, S.; Galbiati, E.; Penaranda-Avila, J.; Brambilla, C.; Tortora, P.; Colombo, M.; Prosperi, D.
    Immobilization of carboxypeptidase from Sulfolobus solfataricus on magnetic nanoparticles improves enzyme stability and functionality in organic media (2014), BMC Biotechnol., 14, 82.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.17.B1

Application

Application Comment Organism
synthesis nanobioconjugate of the enzyme immobilized on silica-coated magnetic nanoparticles exhibits enhanced stability in aqueous media at room temperature as well as in different organic solvents. The improved stability in ethanol paves the way to possible applications of the immobilized enzyme, in particular as a biocatalyst for the synthesis of N-blocked amino acids. Another potential application might be amino acid racemate resolution, a critical and expensive step in chemical synthesis Saccharolobus solfataricus

General Stability

General Stability Organism
immobilization of the enzyme on magnetic nanoparticles improves long-term stability at room temperature compared to the free native enzyme and also results in a significantly higher stability in organic solvents at 40°C Saccharolobus solfataricus

Organic Solvent Stability

Organic Solvent Comment Organism
dimethylformamide the enzyme gradually loses its activity by increasing the dimethylformamide in the solvent mixture, while the nanobioconiugate retains 80% of residual activity even in the presence of 80% dimethylformamide Saccharolobus solfataricus
Ethanol nanobioconjugate of the enzyme immobilized on silica-coated magnetic nanoparticles exhibits enhanced stability in aqueous media at room temperature as well as in different organic solvents. The improved stability in ethanol paves the way to possible applications of immobilized enzyme, in particular as a biocatalyst for the synthesis of N-blocked amino acids Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus P80092
-
-
Saccharolobus solfataricus P2 P80092
-
-

Purification (Commentary)

Purification (Comment) Organism
affinity purification of histidine-tagged enzyme Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoyl-L-arginine + H2O
-
 Saccharolobus solfataricus benzoic acid + L-arginine
-
 ?
benzoyl-L-arginine + H2O
-
 Saccharolobus solfataricus P2 benzoic acid + L-arginine
-
 ?
furylacryloyl-L-phenylalanine + H2O
-
 Saccharolobus solfataricus furylacrylic acid + L-phenylalanine
-
 ?
furylacryloyl-L-phenylalanine + H2O
-
 Saccharolobus solfataricus P2 furylacrylic acid + L-phenylalanine
-
 ?

Synonyms

Synonyms Comment Organism
CPSso
-
 Saccharolobus solfataricus
SSO1355 locus name Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 assay at Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
 the enzyme gradually loses its activity resulting in a complete inactivation after 96 h. The nanobioconjugate of the enzyme immobilized on silica-coated magnetic nanoparticles leads to a substantial increase in stability, up to 85% of initial activity being retained after 96 h Saccharolobus solfataricus
40
-
 in the presence of ethanol at 40°C and various concentrations the inactivation profiles shows that the enzyme has a residual activity of 50% after 6 h, which decreases to 20% after 24 h incubation. The nanobioconjugate of the enzyme immobilized on silica-coated magnetic nanoparticles reveales a significantly improved stability in ethanol at the different tested concentrations compared with free enzyme, up to 80-90% of residual activity after 6 h, and 70% after 24 h incubation in 80% ethanol being retained Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 assay at Saccharolobus solfataricus