纤维素酶
溶菌酶
化学
生物催化
固定化酶
戊二醛
水解
热稳定性
酶
色谱法
化学工程
生物化学
催化作用
有机化学
反应机理
工程类
作者
Qingtai Chen,Dong Liu,Chongchong Wu,Kaisheng Yao,Zhiheng Li,Nan Si,Fusheng Wen,Ian D. Gates
标识
DOI:10.1016/j.biortech.2018.04.071
摘要
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.
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