Characterization of free and immobilized lipase from Penicillium sp. onto three modified bentonites: A comparative study

The present work was conducted to investigate the immobilization of lipase from Penicillium sp. onto three modified bentonites by simple adsorption and crosslinking methods. The composites were characterized by FTIR, SEM and BET. The free and bentonite-supported lipase was evaluated in terms of operational and storage stability and pH and thermal activity and stability. The kinetic parameters were also evaluated. The results show that all immobilized enzymes had better thermal and pH stability compared to free enzymes. Among the immobilized enzymes, GDU-bent-lipase had more efficient performance in thermal (38% of its initial activity within 24 h at 65 degrees C), operational (70% residual activity after 9 cycles), storage stability (70.14% of its initial activities at 4 degrees C for 21 days), and kinetic properties (effectiveness factor 0.79 relative to free enzyme) than free and other immobilized enzymes. The adsorption isotherm was modeled by Langmuir, Freundlich and Temkin isotherms which Langmuir isotherm indicated a better fit of the experimental adsorption data. To the best of our knowledge, this is the first comparative report about the immobilization of lipase Produced by Penicillium sp., isolated from olive mill wastewater, and the most comprehensive study about the immobilization of lipase onto several supports.

Automated summary

This study investigated the immobilization of lipase from Penicillium sp. onto modified bentonites using adsorption and crosslinking methods. The immobilized lipase showed better thermal and pH stability compared to free lipase. Among the immobilized enzymes, GDU-bent-lipase exhibited the most efficient performance in various aspects.