Co-immobilization of cellulase and lysozyme on amino-functionalized magnetic nanoparticles: An activity-tunable biocatalyst for extraction of lipids from microalgae. (September 2018)

• Record Type: Journal Article
• Authors: Chen, Qingtai; Liu, Dong; Wu, Chongchong; Yao, Kaisheng; Li, Zhiheng; Shi, Nan; Wen, Fushan; Gates, Ian D.
• Is Part Of: Bioresource technology. Volume 263(2018)
• Page Start: 317
• Page End: 324
• Publication Date: 2018-09
• Subjects: Co-immobilization -- Magnetic dual-enzyme biocatalyst -- Cellulase -- Lysozyme -- Microalgal lipids extraction; Biomass -- Periodicals; Biomass energy -- Periodicals; Bioremediation -- Periodicals; Agricultural wastes -- Periodicals; Factory and trade waste -- Periodicals; Organic wastes -- Periodicals; Bioénergie -- Périodiques; Déchets agricoles -- Périodiques; Déchets industriels -- Périodiques; Déchets organiques -- Périodiques; Déchets (Combustible) -- Périodiques; 662.88
• DOI: 10.1016/j.biortech.2018.04.071
• Languages: English
• ISSNs: 0960-8524

Abstract

Graphical abstract: Highlights: Cellulase and lysozyme were simultaneous co-immobilized on a given magnetic carrier. Activity-tunable co-immobilized enzymes were used to disrupt microalgae cell walls. Limited active sites caused the competitions between dual-enzyme on a given carrier. Co-immobilized enzymes can be separated from microalgae suspension by using a magnet. Residual activity of co-immobilized enzymes retained up to 60% at six times cycles. Abstract: An activity-tunable biocatalyst for Nannochloropsis sp. cell-walls degradation was prepared by co-immobilization of cellulase and lysozyme on the surface of amino-functionalized magnetic nanoparticles (MNPs) employing glutaraldehyde. The competition between cellulase and lysozyme during immobilization was caused by the limited active sites of the MNPs. The maximum recovery of activities (cellulase: 78.9% and lysozyme: 69.6%) were achieved due to synergistic effects during dual-enzyme co-immobilization. The thermal stability in terms of half-life of the co-immobilized enzymes was three times higher than that in free form and had higher catalytic efficiency for hydrolysis of cell walls. Moreover, the co-immobilized enzymes showed greater thermal stability and wider pH tolerance than free enzymes under harsh conditions. Furthermore, the co-immobilized enzymes retained up to 60% of the residual activity after being recycled 6 times. This study provides a feasible approach for the industrialization of enzyme during cell-walls disruption and lipids extraction from Nannochloropsis sp.