What is the Difference Between Esterase and Lipase?

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Esterase and lipase are both enzymes that hydrolyze ester bonds, but they have distinct differences in their substrate preferences and specificities. Here are the main differences between esterase and lipase:

  1. Substrate Specificity: Lipases are mainly active against water-insoluble substrates, such as triglycerides composed of long-chain fatty acids, whereas esterases preferentially hydrolyze 'simple' esters and usually only triglycerides composed of fatty acids shorter than C6.
  2. Km Value: Esterases and lipases can be differentiated by their value of Km, which is the substrate concentration at which an enzyme reaches half of its maximum reaction rate.
  3. Surface Domain: Lipases, unlike esterases, display a significant difference in the distribution of hydrophobic amino acid residues at the vicinity of the active site, which supports the hypothesis of the existence of a particular surface domain in lipases.
  4. Interfacial Activation: Lipases can be distinguished from esterases by the phenomenon of interfacial activation, which is only observed for lipases.
  5. Organic Solvent Stability: Both enzymes remain stable in organic solvents, but this property is more noticed for lipases.

Comparative Table: Esterase vs Lipase

Esterase and lipase are both enzymes that hydrolyze ester bonds, but they have distinct differences in their substrate preferences and structures. Here is a table comparing the differences between esterase and lipase:

Property Esterase Lipase
Preferred Substrates Short-chain triglycerides, simple esters Long-chain triglycerides, secondary alcohols
Substrate Specificity Less substrate specific, inactive against long-chain fatty acids More substrate specific, active against long-chain fatty acids
Amino Acid Composition Contains more polar amino acids, making them more polar in nature Contains more hydrophobic amino acids, making them more non-polar in nature
Solubility Water-soluble Soluble in organic solvents
Interfacial Activation Not observed Observed
pH-activity Optimum Around 6 Varies depending on the enzyme

Esterases preferentially hydrolyze short-chain triglycerides and simple esters, while lipases are more active against long-chain triglycerides and secondary alcohols. Esterases contain more polar amino acids, making them more polar, whereas lipases have more hydrophobic amino acids, making them more non-polar. Esterases are water-soluble, while lipases are soluble in organic solvents. Interfacial activation is observed in lipases but not in esterases. The pH-activity optimum for esterases is typically around 6, while it varies depending on the lipase enzyme.