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Literature summary for 3.1.1.3 extracted from

  • Bou Ali, M.; Ben Ali, Y.; Karray, A.; Fendri, A.; Gargouri, Y.
    Purification and characterization of the first recombinant bird pancreatic lipase expressed in Pichia pastoris: the turkey (2011), Lipids Health Dis., 10, 24.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.3

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Pichia pastoris strain X33 Meleagris gallopavo

Inhibitors

Inhibitors Comment Organism Structure
sodium deoxycholate recombinant and native enzymes are partially inhibited by the sodium deoxycholate and retain respectively 30 and 25% of their activities at 8 mM Meleagris gallopavo

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ in the absence of CaCl2, the recombinant and native enzymes retain about 10% of their activities. The maximal enzyme activity is measured at 0.5 mM CaCl2 Meleagris gallopavo

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 x * 50000, recombinant enzyme, SDS-PAGE Meleagris gallopavo

Organism

Organism UniProt Comment Textmining
Meleagris gallopavo
-
 turkey
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, DEAE cellulose column chromatography, Sephacryl S200 gel filtration, Q-Sepharose column chromatography, and Sephadex G100 gel filtration Meleagris gallopavo

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
 Meleagris gallopavo
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
399
-
 recombinant enzyme from supernatant, using olive oil as substrate, at pH 8.5, 37°C Meleagris gallopavo
5300
-
 recombinant enzyme after 13.28fold purification, using olive oil as substrate, at pH 8.5, 37°C Meleagris gallopavo
9500
-
 recombinant enzyme after 13.28fold purification, using tributyrin as substrate, at pH 8.5, 37°C Meleagris gallopavo

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme exhibits efficient hydrolysis of oilive oil in the absence of colipase and bile salts Meleagris gallopavo ?
-
 ?
tributyrin + H2O best substrate, efficient hydrolysis in the absence of colipase and bile salts Meleagris gallopavo dibutyrin + butyrate
-
 ?

Subunits

Subunits Comment Organism
? x * 50000, recombinant enzyme, SDS-PAGE Meleagris gallopavo

Synonyms

Synonyms Comment Organism
TPL
-
 Meleagris gallopavo
triacylglycerol acylhydrolase
-
 Meleagris gallopavo

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 recombinant enzyme Meleagris gallopavo

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
55
-
 at 55°C, the recombinant and native enzyme keep 75% and 85% of their activity respectively. Up to 55°C, the two enzymes retain only 10% of their activities Meleagris gallopavo

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50 60 the recombinant and native enzymes retain 80% and 95% of their activity, respectively, after 30 min of incubation at 50°C. At temperature over 55°C, the activity decreaseds dramatically to reach 15 to 20% for both enzymes at 60°C Meleagris gallopavo

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 recombinant enzyme Meleagris gallopavo

pH Stability

pH Stability pH Stability Maximum Comment Organism
8 9 the recombinant and native enzymes keep 100% of their activity after 30 min incubation at pH 8.0 and 9.0. When incubated at pH 3, both enzymes retain 70% of their activities Meleagris gallopavo