What is the Difference Between Esterase and Lipase?
🆚 Go to Comparative Table 🆚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:
- 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.
- 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.
- 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.
- Interfacial Activation: Lipases can be distinguished from esterases by the phenomenon of interfacial activation, which is only observed for lipases.
- 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.
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