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Alpha-l-arabinofuranosidase from Rhodotorula flava | JoVE Visualize

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Alpha-l-arabinofuranosidase from Rhodotorula flava

E Uesaka, M Sato, M Raiju

Journal of Bacteriology|March 1, 1978

View abstract on PubMed

Summary

A novel alpha-L-arabinofuranosidase from Rhodotorula flava exhibits remarkable stability at low pH. This enzyme shows high activity and stability, making it a promising candidate for industrial applications requiring acidic conditions.

Area of Science:

Enzymology
Microbiology
Biochemistry

Background:

Alpha-L-arabinofuranosidases are crucial enzymes for degrading arabinan polysaccharides.
Investigating microbial enzymes offers potential for novel biocatalysts.
Rhodotorula flava is a yeast species with potential for producing industrial enzymes.

Purpose of the Study:

To highly purify and characterize an alpha-L-arabinofuranosidase from Rhodotorula flava.
To assess the enzyme's stability and kinetic properties under acidic conditions.

Main Methods:

Enzyme purification from the culture fluid of Rhodotorula flava.
Determination of pH optimum and acid stability.
Kinetic analysis using phenyl alpha-L-arabinofuranoside as substrate.

Main Results:

The purified enzyme demonstrated a pH optimum of 2.0.
The enzyme retained 82% activity after 24 hours at pH 1.5 and 30°C, indicating unusual acid stability.
Apparent Km and Vmax values were 9.1 mM and 72.5 µmol/min/mg protein, respectively.

Conclusions:

Rhodotorula flava produces a highly acid-stable alpha-L-arabinofuranosidase.
The enzyme's properties suggest potential applications in industries requiring acidophilic biocatalysis.
Further research could explore its use in biomass processing or food industries.

Aerospace Engineering

Alpha-l-arabinofuranosidase From Rhodotorula Flava