Mannanase transfer into hexane and xylene by liquid-liquid extraction

Area of Science:

• Biochemistry
• Enzyme catalysis
• Biotechnology

Background:

• Enzymes typically function in aqueous environments.
• Protein transfer into organic solvents is challenging.
• Ionic surfactants can modify protein properties.

Purpose of the Study:

• To investigate the formation of noncovalent complexes between glycosidase, endo-1,4-beta-D-mannanase, and AOT.
• To promote protein transfer into organic solvents like xylene and hexane.
• To evaluate the catalytic activity of mannanase in these organic media.

Main Methods:

• Formation of noncovalent complexes between mannanase and AOT.
• Solubilization of enzyme-surfactant complexes in hexane and xylene.
• Assay of enzyme catalytic activity in organic solvents.

Main Results:

• Mannanase was solubilized in hexane (≥2.5 mg/ml) and xylene (≥2.0 mg/ml) via complexation with AOT.
• Enzyme activity in hexane increased with AOT concentration, reaching ~10% of aqueous activity.
• In xylene, enhanced activity was observed at 0.1-0.3 mg/ml mannanase; higher concentrations showed negligible activity.

Conclusions:

• Noncovalent complexation with AOT facilitates mannanase transfer and activity in organic solvents.
• The concentration of both enzyme and surfactant is critical for achieving optimal activity in xylene.
• This approach offers potential for enzymatic applications in non-aqueous systems.