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Literature summary extracted from

  • Chakraborty, K.; Raj, R.P.
    An extra-cellular alkaline metallolipase from Bacillus licheniformis MTCC 6824: Purification and biochemical characterization (2008), Food Chem., 109, 727-736.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.3 sorbitol a combination of Ca2+ and sorbitol induces a synergistic effect on the activity of lipase with a significantly high residual activity (100%), even after 45 min, as compared to 91.5% when incubated with Ca2+ alone Bacillus licheniformis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.3 2-mercaptoethanol
-
Bacillus licheniformis
3.1.1.3 acetonitrile inhibitory at 5% (v/v) Bacillus licheniformis
3.1.1.3 chloroform inhibitory at 3% (v/v) Bacillus licheniformis
3.1.1.3 Co2+ 82.7% inhibition at 50 mM Bacillus licheniformis
3.1.1.3 Cu2+ 31% inhibition at 10 mM Bacillus licheniformis
3.1.1.3 EDTA significant inhibition at 70 mM Bacillus licheniformis
3.1.1.3 ethyl acetate inhibitory at 8% (v/v) Bacillus licheniformis
3.1.1.3 Fe2+ 33% inhibition at 10 mM Bacillus licheniformis
3.1.1.3 Hg2+ 72% inhibition at 70 mM Bacillus licheniformis
3.1.1.3 additional information Na+ has no significant effect on the enzyme activity; the activity is strongly affected by the thiol inhibitor N-bromosuccinimide Bacillus licheniformis
3.1.1.3 phenylmethylsulfonyl fluoride completely inactivates the original lipase at 70 mM Bacillus licheniformis
3.1.1.3 Zn2+ 69.1% inhibition at 50 mM Bacillus licheniformis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.3 9.3
-
triolein at 45°C Bacillus licheniformis
3.1.1.3 12
-
tristearin at 45°C Bacillus licheniformis
3.1.1.3 15
-
tripalmitin at 45°C Bacillus licheniformis
3.1.1.3 22
-
trilaurin at 45°C Bacillus licheniformis
3.1.1.3 29
-
4-nitrophenyl palmitate at 45°C Bacillus licheniformis
3.1.1.3 34
-
tributyrin at 45°C Bacillus licheniformis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.3 Ca2+ the catalytic activity is enhanced by Ca2+ (18%) at 30 mM and higher concentrations Bacillus licheniformis
3.1.1.3 Mg2+ the catalytic activity is enhanced by Mg2+ (12%) at 30 mM and higher concnetrations Bacillus licheniformis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.3 74800
-
apparent molecular mass, non-denaturing PAGE Bacillus licheniformis

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
3.1.1.3 isopropanol relative activity of 62% is apparent in the presence of 1% (v/v) isopropanol Bacillus licheniformis
3.1.1.3 Methanol relative activity of 71% is apparent in the presence of 1% (v/v) methanol Bacillus licheniformis

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Bacillus licheniformis
-
-
-
3.1.1.3 Bacillus licheniformis MTCC 6824
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.3 ammonium sulfate fractionation, ethanol/ether precipitation, dialysis, Amberlite IRA 410 chromatography, and Sephadex G 100 gel filtration Bacillus licheniformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 4-nitrophenyl palmitate + H2O
-
Bacillus licheniformis 4-nitrophenol + palmitate
-
?
3.1.1.3 4-nitrophenyl palmitate + H2O
-
Bacillus licheniformis MTCC 6824 4-nitrophenol + palmitate
-
?
3.1.1.3 glyceryl trioleate + 3 H2O 14% activity compared to glyceryl tributyrate Bacillus licheniformis glycerol + 3 oleate
-
?
3.1.1.3 glyceryl trioleate + 3 H2O 14% activity compared to glyceryl tributyrate Bacillus licheniformis MTCC 6824 glycerol + 3 oleate
-
?
3.1.1.3 tributyrin + 3 H2O 100% activity Bacillus licheniformis glycerol + 3 butyrate
-
?
3.1.1.3 tributyrin + 3 H2O 100% activity Bacillus licheniformis MTCC 6824 glycerol + 3 butyrate
-
?
3.1.1.3 trilaurin + 3 H2O 66% activity compared to glyceryl tributyrate Bacillus licheniformis glycerol + 3 laurate
-
?
3.1.1.3 trilaurin + 3 H2O 66% activity compared to glyceryl tributyrate Bacillus licheniformis MTCC 6824 glycerol + 3 laurate
-
?
3.1.1.3 triolein + H2O
-
Bacillus licheniformis 1,2-diolein + oleate
-
?
3.1.1.3 triolein + H2O
-
Bacillus licheniformis MTCC 6824 1,2-diolein + oleate
-
?
3.1.1.3 tripalmitin + 3 H2O 42% activity compared to glyceryl tributyrate Bacillus licheniformis glycerol + 3 palmitate
-
?
3.1.1.3 tristearin + 3 H2O 31% activity compared to glyceryl tributyrate Bacillus licheniformis glycerol + 3 stearate
-
?

Subunits

EC Number Subunits Comment Organism
3.1.1.3 monomer 1 * 74800, non-denaturing PAGE Bacillus licheniformis

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 triacylglycerol acyl hydrolase
-
Bacillus licheniformis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 45
-
-
Bacillus licheniformis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.3 45 65 half-lives of 82 min at 45°C and 48 min at 55°C, the activity is reduced to 63.9% of its original value in 20 min at 50°C, the enzyme retains 81.9% of the residual activity after 60 min of incubation at 45°C, and 69.3% after 2 h, at higher temperatures, e.g. 50 and 55°C, the lipase exhibits 69% and 59% of the maximum activity after 1 h of incubation, and 43% and 32% of the residual activity after 2 h of incubation, lipase exhibits significant activity even at 65°C (48% of the residual activity) after 1 h of incubation Bacillus licheniformis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 8
-
-
Bacillus licheniformis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.3 6 10
-
Bacillus licheniformis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.3 3 11 67.9% activity at pH 9.0, 22.6% activity at pH 10.0, the activity is reduced drastically at pH 5.0 (15.5%) and is 1.94% of the maximum at pH 11.0, the enzyme is inactivated at acidic pH (4.0) losing 97.0% of its original activity, at pH 3.0, the enzyme loses about 99.7% of its initial activity Bacillus licheniformis