首页> 外文期刊>Bioresource Technology: Biomass, Bioenergy, Biowastes, Conversion Technologies, Biotransformations, Production Technologies >Co-immobilization of cellulase and lysozyme on amino-functionalized magnetic nanoparticles: An activity-tunable biocatalyst for extraction of lipids from microalgae
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Co-immobilization of cellulase and lysozyme on amino-functionalized magnetic nanoparticles: An activity-tunable biocatalyst for extraction of lipids from microalgae

机译:氨基官能化磁性纳米粒子纤维素酶和溶菌酶的共同固定:一种用于萃取微藻脂质的活性可调生物催化剂

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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.
机译:用于Nannchloropsis sp的活性可调生物催化剂。通过在氨基官能化磁性纳米颗粒(MNP)表面上的纤维素酶和溶菌酶的共同固定来制备细胞壁降解氨基官能化磁性纳米颗粒(MNP)的溶氨基醛。固定过程中纤维素酶和溶菌酶之间的竞争是由MNP的有限活性位点引起的。由于双酶共固化期间,实现了活性的最大回收率(纤维素酶:78.9%和溶菌酶:69.6%)。在共固化酶的半衰期方面的热稳定性比以自由形式的半衰期高三倍,并且对细胞壁的水解具有更高的催化效率。此外,共固定化酶在恶劣条件下的游离酶比游离酶更大的热稳定性和更宽的pH耐受性。此外,在再循环6次后,共固化酶保留高达60%的残留活性。本研究提供了一种可行的方法,用于在纳米氯磺酸盐液中的细胞壁破坏和脂质中酶的产业化方法。

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