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BRENDA support

Literature summary for 3.1.1.3 extracted from

  • Branco, R.V.; Gutarra, M.L.; Guisan, J.M.; Freire, D.M.; Almeida, R.V.; Palomo, J.M.
    Improving the thermostability and optimal temperature of a lipase from the hyperthermophilic archaeon Pyrococcus furiosus by covalent immobilization (2015), Biomed Res. Int., 2015, 250532.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus Q8TZJ1
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl butyrate + H2O
-
Pyrococcus furiosus 4-nitrophenol + butyrate
-
?

Synonyms

Synonyms Comment Organism
Pf2001DELTA60
-
Pyrococcus furiosus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
66
-
enzyme immobilized on octyl-agarose or glyoxyl agarose Pyrococcus furiosus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
66 90 66°C: optimum, 90°C: enzyme immobilized on glyoxyl agaroseis active at 90°C Pyrococcus furiosus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
thermostability of the enzyme immobilized on different supports. The highest enzyme stability after 48 h incubation at 70°C is achieved with immobilization on glyoxylagarose (82%). The enzyme immobilized on this support in the presence of DTT at pH 7 maintains around 69% activity. The immobilization of the enzyme on octyl-agarose (interfacially activated), yields the worst lipase biocatalyst (27% remaining activity) Pyrococcus furiosus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
enzyme immobilized on octyl-agarose or glyoxyl agarose Pyrococcus furiosus