Development of a Sustainable Biocatalytic Process for Geranyl Benzoate Production Using Immobilized Lipase

Area of Science:

• Biocatalysis
• Green Chemistry
• Enzyme Engineering

Background:

• Growing demand for sustainable and natural ingredients in flavor and fragrance industries.
• Enzymatic synthesis presents a viable alternative to traditional chemical routes.
• Geranyl benzoate, a monoterpenoid ester, has potential bioactivity and commercial applications.

Purpose of the Study:

• To optimize the enzymatic production of geranyl benzoate using immobilized lipases in a solvent-free system.
• To investigate the impact of process variables and byproducts on enzyme performance and reaction efficiency.
• To assess the cytotoxicity and proliferative effects of geranyl benzoate.

Main Methods:

• Immobilized lipases (Lipozyme 435) were used for esterification in a solvent-free system.
• Central composite design was employed to optimize molar ratio, temperature, and enzyme loading.
• Inhibitory effects of methanol and methyl benzoate were evaluated; enzyme reusability and cytotoxicity were assessed.

Main Results:

• Optimal conditions (1:7 molar ratio, 80°C, 30% enzyme) yielded 72% geraniol conversion in 6 hours.
• Open-reactor systems significantly enhanced conversion (>99% in 48 h) by enabling methanol evaporation.
• Methyl benzoate inhibited Lipozyme 435 activity by 54%, while Lipura Flex showed higher resilience; Lipozyme 435 retained 22% activity after five cycles.

Conclusions:

• Solvent-free enzymatic processes are promising for sustainable geranyl benzoate production.
• Effective methanol management and strategies to enhance biocatalyst stability are crucial for industrial scalability.
• Geranyl benzoate exhibited no cytotoxicity and a proliferative effect at high concentrations.