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Molecules 2016, 21(8), 972; doi:10.3390/molecules21080972

Immobilization of Chlamydomonas reinhardtii CLH1 on APTES-Coated Magnetic Iron Oxide Nanoparticles and Its Potential in the Production of Chlorophyll Derivatives

1
Institute of Genomics and Bioinformatics, National Chung Hsing University, Taichung 40227, Taiwan
2
Agricultural Biotechnology Center, National Chung Hsing University, Taichung 40227, Taiwan
3
Institute of Biomedical Engineering and Nanomedicine, National Health Research Institutes, Miaoli 35053, Taiwan
4
Institute of Plant and Microbial Biology, Academia Sinica, Taipei 11529, Taiwan
5
Department of Biological Science & Technology, I-Shou University, Kaohsiung 840, Taiwan
*
Authors to whom correspondence should be addressed.
Academic Editor: Steven Bull
Received: 25 June 2016 / Revised: 18 July 2016 / Accepted: 21 July 2016 / Published: 26 July 2016
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Abstract

Recombinant Chlamydomonas reinhardtii chlorophyllase 1 (CrCLH1) that could catalyze chlorophyll hydrolysis to chlorophyllide and phytol in vitro was successfully expressed in Escherichia coli. The recombinant CrCLH1 was immobilized through covalent binding with a cubic (3-aminopropyl) triethoxysilane (APTES) coating on magnetic iron oxide nanoparticles (MIONPs), which led to markedly improved enzyme performance and decreased biocatalyst costs for potential industrial application. The immobilized enzyme exhibited a high immobilization yield (98.99 ± 0.91 mg/g of gel) and a chlorophyllase assay confirmed that the immobilized recombinant CrCLH1 retained enzymatic activity (722.3 ± 50.3 U/g of gel). Biochemical analysis of the immobilized enzyme, compared with the free enzyme, showed higher optimal pH and pH stability for chlorophyll-a hydrolysis in an acidic environment (pH 3–5). In addition, compared with the free enzyme, the immobilized enzyme showed higher activity in chlorophyll-a hydrolysis in a high temperature environment (50–60 °C). Moreover, the immobilized enzyme retained a residual activity of more than 64% of its initial enzyme activity after 14 cycles in a repeated-batch operation. Therefore, APTES-coated MIONP-immobilized recombinant CrCLH1 can be repeatedly used to lower costs and is potentially useful for the industrial production of chlorophyll derivatives. View Full-Text
Keywords: Chlamydomonas reinhardtii chlorophyllase 1; immobilized enzyme; magnetic iron oxide nanoparticles; chlorophyll derivatives Chlamydomonas reinhardtii chlorophyllase 1; immobilized enzyme; magnetic iron oxide nanoparticles; chlorophyll derivatives
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Yen, C.-C.; Chuang, Y.-C.; Ko, C.-Y.; Chen, L.-F.O.; Chen, S.-S.; Lin, C.-J.; Chou, Y.-L.; Shaw, J.-F. Immobilization of Chlamydomonas reinhardtii CLH1 on APTES-Coated Magnetic Iron Oxide Nanoparticles and Its Potential in the Production of Chlorophyll Derivatives. Molecules 2016, 21, 972.

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