Enhanced triolein and ethyl ferulate interesterification performance by CRL-AuNPs

Area of Science:

• Biocatalysis
• Enzyme Engineering
• Nanotechnology

Background:

• Candida rugosa lipase (CRL) is a key enzyme for esterification reactions.
• Improving enzyme activity and stability is crucial for industrial biocatalysis.
• Gold nanoparticles (AuNPs) can enhance enzyme performance.

Purpose of the Study:

• To develop an optimized Candida rugosa lipase-gold nanoparticle (CRL-AuNPs) system.
• To investigate the effect of different preparation methods on CRL-AuNPs activity and hybridization efficiency.
• To evaluate the stability of the optimized CRL-AuNPs system.

Main Methods:

• Interesterification of triolein and ethyl ferulate catalyzed by CRL.
• Molecular docking to predict substrate-enzyme binding modes.
• Preparation and characterization of CRL-AuNPs using varying gold nanoparticle concentrations and molar ratios.
• Enzyme activity assays and stability tests.

Main Results:

• Optimized CRL-AuNPs preparation (molar ratio of Mb to HAuCl4 of 0.2) enhanced enzyme activity to 5.98 U/mg and achieved 71.8% hybridization efficiency.
• The optimized CRL-AuNPs system retained 95% activity after 6 repetitions and 85.6% after 30 days at room temperature.
• Different preparation methods significantly impacted CRL activity and AuNPs hybridization efficiency.

Conclusions:

• The optimized CRL-AuNPs system offers enhanced biocatalytic activity and stability compared to native CRL.
• This study presents a promising approach for developing robust enzymatic systems for interesterification.
• The findings suggest significant potential for CRL-AuNPs in industrial applications requiring efficient and stable lipases.