Microbial lipase: a new approach for a heterogeneous biocatalyst

Area of Science:

• Biotechnology
• Enzyme Engineering

Background:

• Lipases are crucial industrial enzymes.
• Enzyme immobilization enhances stability and reusability.
• Hydrophobic interaction is a viable immobilization strategy.

Purpose of the Study:

• To immobilize lipase from Aspergillus sp. using hydrophobic interaction.
• To evaluate the stability and reusability of the immobilized lipase.

Main Methods:

• Submerged cultivation of Aspergillus sp. to produce lipase.
• Lipase immobilization onto octyl-sepharose (C8) and octadecyl-sepabeads (C18) carriers via hydrophobic interaction.
• Removal of excess oil from the fermented broth prior to immobilization.
• Multiple immobilization cycles to enhance enzyme loading.
• Enzyme activity and stability assays.

Main Results:

• Successful immobilization of lipase onto C8 and C18 carriers.
• Octyl-sepharose concentrated the enzyme with 22% initial activity.
• Four immobilization cycles yielded 151.32% immobilization yield.
• Specific activity increased by 136% after immobilization.
• Immobilized lipase retained 75% of initial activity after 20 reuse cycles.

Conclusions:

• Hydrophobic interaction is effective for lipase immobilization.
• Immobilized lipase exhibits enhanced stability and reusability for industrial processes.
• This approach increases enzyme efficiency and reduces operational costs.