Alcohol dehydrogenase from Rhizopus javanicus.

Area of Science:

• Biochemistry
• Enzymology
• Microbial Biotechnology

Background:

• Alcohol dehydrogenase (ADH) plays a crucial role in microbial metabolism.
• Understanding the properties of ADH from various sources is important for biotechnological applications.
• Rhizopus javanicus is a fungus known to produce various enzymes.

Purpose of the Study:

• To purify and characterize the alcohol dehydrogenase from Rhizopus javanicus.
• To determine the molecular weight and subunit composition of the enzyme.
• To investigate the presence of multiple enzyme forms in the crude extract.

Main Methods:

• Enzyme purification techniques.
• Determination of molecular weight using methods like gel filtration or SDS-PAGE.
• Ion-exchange chromatography for separating enzyme isoforms.

Main Results:

• Purification of alcohol dehydrogenase from Rhizopus javanicus.
• The intact enzyme has a molecular weight of approximately 60,000 Da.
• The enzyme is composed of four subunits, each with an apparent molecular weight of 14,000 Da.
• Multiple forms of alcohol dehydrogenase were detected and separated from the crude mycelial extract.

Conclusions:

• Alcohol dehydrogenase from Rhizopus javanicus is a tetrameric enzyme.
• The characterization provides fundamental data for potential enzymatic applications.
• The presence of multiple forms suggests complex regulation or post-translational modifications.