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Literature summary extracted from

  • Park, K.M.; Kwon, O.T.; Ahn, S.M.; Lee, J.; Chang, P.S.
    Characterization and optimization of carboxylesterase-catalyzed esterification between capric acid and glycerol for the production of 1-monocaprin in reversed micellar system (2010), New Biotechnol., 27, 46-52.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.1.1 synthesis the enzyme is useful for the synthesis of 1-monocaprin, a widely used functional emulsifier in the food, cosmetic, and pharmaceutical industries and is recognized as a GRAS food additive Calotropis procera

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.1 additional information carboxylesterase is solubilized in reversed micellar glycerol droplets containing a very small amount of water and stabilized by a surfactant bis(2-ethylhexyl) sodium sulfosuccinate, optimization of carboxylesterase-catalyzed esterification between capric acid and glycerol for the production of 1-monocaprin in the reversed micellar system Calotropis procera

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.1 Co2+ 18% inhibition at 25 mM Calotropis procera
3.1.1.1 Cu2+ over 94% inhibition at 25 mM Calotropis procera
3.1.1.1 Fe2+ 97% inhibition at 25 mM Calotropis procera
3.1.1.1 Sn2+ 63% inhibition at 25 mM Calotropis procera
3.1.1.1 Zn2+ 46% inhibition at 25 mM Calotropis procera

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.1 additional information
-
 additional information the carboxylesterase-catalyzed esterification of capric acid in the reversed micellar system follows Michaelis-Menten kinetics Calotropis procera
3.1.1.1 9.64
-
 capric acid pH 10.0, 60°C Calotropis procera

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.1 extracellular latex Calotropis procera
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.1 Calotropis procera
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.1 native enzyme partially from latex by ammonium sulfate fractionation and dialysis Calotropis procera

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.1 latex from stems and leaves Calotropis procera
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.1 capric acid + sn-glycerol the carboxylesterase performs also the esterification reaction using capric acid and glycerol as substrates resulting in formation of 1-monocaprin, product analysis by HPLC and method optimization, overview Calotropis procera 1-monocaprin
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.1 60
-
-
 Calotropis procera

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.1 10
-
-
 Calotropis procera