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Extracellular RNase produced by Yarrowia lipolytica
Journal of Bacteriology
|November 1, 1986
Summary
Yarrowia lipolytica secretes a single extracellular ribonuclease (RNase). This enzyme undergoes degradation, forming smaller RNases, primarily influenced by alkaline protease activity.
Area of Science:
- Microbiology
- Enzymology
- Biochemistry
Background:
- Yarrowia lipolytica is known to produce extracellular enzymes.
- Understanding the specific enzymes secreted and their properties is crucial for biotechnological applications.
Purpose of the Study:
- To investigate the production and characteristics of extracellular ribonuclease (RNase) secreted by Yarrowia lipolytica.
- To identify the different RNase forms and elucidate their relationship.
Main Methods:
- Cultivation of Yarrowia lipolytica CX161-1B in varying pH media.
- Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for molecular weight determination.
- Enzyme purification and characterization, including gel filtration and isoelectric focusing.
Main Results:
- Y. lipolytica secretes a 45,000-molecular-weight RNase.
- Smaller RNases (43,000 and 34,000 MW) are degradation products of the 45,000 MW RNase.
- Alkaline extracellular protease plays a key role in RNase degradation.
- The purified RNase is a glycoprotein with a pH optimum of 6.5-7.0.
Conclusions:
- Y. lipolytica produces a single primary extracellular RNase.
- Enzymatic degradation significantly affects the observed RNase profile.
- The characterized RNase is a glycoprotein with specific activity at neutral pH.