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Literature summary for 3.1.1.3 extracted from

  • Khurana, J.; Singh, R.; Kaur, J.
    Engineering of Bacillus lipase by directed evolution for enhanced thermal stability: effect of isoleucine to threonine mutation at protein surface (2011), Mol. Biol. Rep., 38, 2919-2926.
    View publication on PubMed
Search for more literature for 3.1.1.3

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli M15 cells Bacillus sp. (in: Bacteria)

Protein Variants

Protein Variants Comment Organism
I56T the mutant shows 3fold improved thermostability at 50°C compared to the wild type enzyme, the specific activity of the mutant enzyme is enhanced approximately twice in comparison to wild type with preference for long chain triacylglycerols Bacillus sp. (in: Bacteria)

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24000
-
 x * 24000, SDS-PAGE Bacillus sp. (in: Bacteria)

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
-
-
-

Purification (Commentary)

Purification (Comment) Organism
mutant enzyme I56T is purified by Ni-NTA column chromatography Bacillus sp. (in: Bacteria)

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
32
-
 wild type enzyme from culture supernatant, pH 8.0, 37°C Bacillus sp. (in: Bacteria)
3170
-
 mutant enzyme I56T from culture supernatant, pH 8.0, 37°C Bacillus sp. (in: Bacteria)
5834
-
 mutant enzyme I56T after 208fold purification, pH 8.0, 37°C Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl acetate + H2O about 45% activity compared to 4-nitrophenyl butyrate Bacillus sp. (in: Bacteria) 4-nitrophenol + acetate
-
 ?
4-nitrophenyl butyrate + H2O best substrate for wild type enzyme Bacillus sp. (in: Bacteria) 4-nitrophenol + butyrate
-
 ?
4-nitrophenyl decanoate + H2O about 100% activity compared to 4-nitrophenyl butyrate Bacillus sp. (in: Bacteria) 4-nitrophenol + decanoate
-
 ?
4-nitrophenyl laurate + H2O about 80% activity compared to 4-nitrophenyl butyrate Bacillus sp. (in: Bacteria) 4-nitrophenol + laurate
-
 ?
4-nitrophenyl myristate + H2O about 30% activity compared to 4-nitrophenyl butyrate Bacillus sp. (in: Bacteria) 4-nitrophenol + myristate
-
 ?
4-nitrophenyl palmitate + H2O about 30% activity compared to 4-nitrophenyl butyrate Bacillus sp. (in: Bacteria) 4-nitrophenol + palmitate
-
 ?
4-nitrophenyl stearate + H2O about 15% activity compared to 4-nitrophenyl butyrate Bacillus sp. (in: Bacteria) 4-nitrophenol + stearate
-
 ?

Subunits

Subunits Comment Organism
? x * 24000, SDS-PAGE Bacillus sp. (in: Bacteria)

Synonyms

Synonyms Comment Organism
lipase
-
 Bacillus sp. (in: Bacteria)
triacylglycerol acylhydrolase
-
 Bacillus sp. (in: Bacteria)

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
33
-
 wild type enzyme Bacillus sp. (in: Bacteria)
38
-
 mutant enzyme I56T Bacillus sp. (in: Bacteria)

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 the wild type enzyme shows a half-life of 7 min at 50°C, the mutant enzyme I567T shows a half-life of 21 min at 50°C Bacillus sp. (in: Bacteria)

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Bacillus sp. (in: Bacteria)

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 8 mutant enzyme I56T Bacillus sp. (in: Bacteria)
7 10 wild type enzyme Bacillus sp. (in: Bacteria)