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Lipases immobilized on the modified polyporous magnetic cellulose support as an efficient and recyclable catalyst for biodiesel production from Yellow horn seed oil

In the present study, modified polyporous magnetic cellulose beads (PMCBs) were synthesized by several organic amines (EDA, DETA, TETA and AST) grafting PMCBs and then utilized as a new kind of support to immobilize Candida antarctica lipase B (CALB) for biodiesel production. The immobilized lipase...

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Bibliographic Details
Published in:Renewable energy 2020-01, Vol.145, p.1246-1254
Main Authors: Zhang, Huaxia, Liu, Tianshu, Zhu, Yawei, Hong, Li, Li, Tianfeng, Wang, Xiqing, Fu, Yujie
Format: Article
Language:English
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Summary:In the present study, modified polyporous magnetic cellulose beads (PMCBs) were synthesized by several organic amines (EDA, DETA, TETA and AST) grafting PMCBs and then utilized as a new kind of support to immobilize Candida antarctica lipase B (CALB) for biodiesel production. The immobilized lipase catalysts based on PMCBs were characterized by Fourier transform infrared and scanning electron microscopy. The results showed that PMCBs-DETA was a more suitable immobilization support and the catalytic activity of immobilized lipases could reach 1.0 U/mg. Then the synthesized catalyst of CALB-PMCBs-DETA was used to produce biodiesel from Yellow horn seed oil via transesterification reaction. A high biodiesel yield (92.3%) was obtained under the optimal reaction conditions and the main compositions of the prepared biodiesel were tested by GC-MS. Moreover, the catalyst of CALB-PMCBs-DETA could be removed easily by a magnet and recycled at least 5 times. As a new kind of support, the modified PMCBs could be a promising alternative for the carriers of immobilizing enzymes used for the green and efficient production of biodiesel. [Display omitted] •PMCBs were modified by grafting amines and CALB was immobilized on the modified support materials for the first time.•The synthesized catalyst of CALB-PMCBs-DETA could be removed from the reaction system easily by a magnet.•This study provide a promising alternative for the carriers of immobilizing enzymes.
ISSN:0960-1481
1879-0682
DOI:10.1016/j.renene.2019.06.031