What is the Difference Between Proteinase K and Protease?
🆚 Go to Comparative Table 🆚Proteinase K and protease are both protein-cleaving enzymes, but they differ in their specific functions and applications. Here are the main differences between the two:
- Substrate specificity: Proteinase K is a broad-spectrum serine protease that mainly acts on keratin protein and is used for digesting proteins and eliminating contamination from nucleic acid preparations. In contrast, protease is a general term for enzymes that catalyze proteolysis, and it acts mainly on the proteins in food, playing a key role in biological functions such as digestion of ingested proteins, protein catabolism, and cell signaling.
- Type of protease: Proteinase K is a subtilisin-type protease, which cleaves at the carboxyl side of hydrophobic, aliphatic, and aromatic amino acids. Proteases, on the other hand, are a class of enzymes that cleave peptide bonds in proteins and include various types such as serine proteases, cysteine proteases, and metalloproteases.
- Applications: Proteinase K is commonly used in molecular biology and biochemistry applications to digest proteins and remove nucleases that can degrade DNA and RNA. It is also used in the isolation of intact genomic DNA from various sources. Proteases, in general, are involved in many biological processes, including protein degradation, blood coagulation, and digestion.
- Temperature and pH stability: Proteinase K possesses a high specific activity over a wide range of temperatures and pH values, and soluble calcium is not essential for its enzymatic activity. In contrast, proteases can have varying temperature and pH stabilities, depending on the specific type of protease.
On this pageWhat is the Difference Between Proteinase K and Protease? Comparative Table: Proteinase K vs Protease
Comparative Table: Proteinase K vs Protease
Proteinase K and protease are both protein-cleaving enzymes, but they differ in their specificity and applications. Here is a table highlighting the differences between the two:
| Feature | Proteinase K | Protease |
|---|---|---|
| Type | Broad-spectrum serine protease | Enzyme catalyzing proteolysis |
| Origin | Fungus Engyodontium album species | Various sources, depending on the specific protease |
| Substrate Specificity | Cleaves at the carboxyl side of hydrophobic, aliphatic, and aromatic amino acids | Acts mainly on proteins in foods and plays a key role in multiple biological functions, such as digestion of ingested proteins and protein catabolism |
| Applications | Used during DNA and RNA preparation for protease digestion, as well as for digesting proteins and eliminating contamination from nucleic acid preparations | Useful in biological functions, such as digestion of ingested proteins, protein catabolism, and cell signaling |
| Inhibition | Soluble calcium is not essential for enzymatic activity, and EDTA cannot inhibit Proteinase K activity | Heat-inactivated by incubation at 95°C for 10 minutes |
Proteinase K is a subtilisin-type protease that is particularly suitable for short digestion times and has a high specific activity over a wide range of temperatures and pH values. In contrast, protease is a more general term for enzymes that catalyze proteolysis and play a role in various biological functions.
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