ArticleMolecules (Basel, Switzerland)2015
Purification and immobilization of the recombinant Brassica oleracea Chlorophyllase 1 (BoCLH1) on DIAION®CR11 as potential biocatalyst for the production of chlorophyllide and phytol.
Article in Molecules (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 14 citations in OpenAlex.
- How to Enhance the Applicability of Metal Ion Affinity-bound Biocatalysts? Comprehensive Overview and Case Study With a Phenylalanine Ammonia Lyase and an Amine Transaminase.Chembiochem : a European journal of chemical biology · 2026Article
- Potential α-glucosidase inhibitors from cultures of Biscogniauxia capnodes SWUF15-40 fungus.Journal of natural medicines · 2025Article
- Chlorophyllides: Preparation, Purification, and Application.Biomolecules · 2021Review
- Co-immobilized recombinant glycosyltransferases efficiently convert rebaudioside A to M in cascade.RSC advances · 2021Article
- Cytotoxic Effects of Chlorophyllides in Ethanol Crude Extracts from Plant Leaves.Evidence-based complementary and alternative medicine : eCAM · 2019Article
- Immobilization of Chlamydomonas reinhardtii CLH1 on APTES-Coated Magnetic Iron Oxide Nanoparticles and Its Potential in the Production of Chlorophyll Derivatives.Molecules (Basel, Switzerland) · 2016Article
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5 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Recombinant Brassica oleracea chlorophyllase 1 (BoCLH1) with a protein molecular weight of 38.63 kDa was successfully expressed in E. coli and could catalyze chlorophyll (Chl) hydrolysis to chlorophyllide and phytol in vitro. In this study, we used DIAION®CR11, a highly porous cross-linked polystyrene divinylbenzene-based metal chelator, for purifying and immobilizing the poly (His)-tagged enzyme. The Cu(II) showed the highest protein adsorption (9.2 ± 0.43 mg/g gel) and enzyme activity (46.3 ± 3.14 U/g gel) for the immobilization of the poly (His)-tagged recombinant BoCLH1 compared with other metal chelators. Biochemical analysis of the immobilized enzyme showed higher chlorophyllase activity for Chl a hydrolysis in a weak base environment (pH 8.0), and activity above 70% was in a high-temperature environment, compared with the free enzyme. In addition, compared with free BoCLH1, the enzyme half-life (t1/2) of the immobilized BoCLH1 increased from 25.42 to 54.35 min (approximately two-fold) at 60 °C. The immobilized enzyme retained a residual activity of approximately 60% after 17 cycles in a repeated-batch operation. Therefore, DIAION®CR11Cu(II)-immobilized recombinant BoCLH1 can be repeatedly used to lower the cost and is potentially useful for the industrial production of chlorophyllide and phytol.
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