Catalytic Activity and Application of Immobilized Chloroperoxidase by Biometric Magnetic Nanoparticles

Abstract

A novel immobilization method for chloroperoxidase (CPO) via carbohydrate-binding lectin protein, concanavalin A (ConA), was investigated. ConA was attached on the surface of silica-coated magnetic nanoparticles (MNPs) for effective recovery. CPO showed ∼100% activity recovery after its immobilization on ConA functionalized MNPs. After storing for four weeks, the immobilized CPO still maintained 80% activity while only 46% of activity of free enzyme was retained. Immobilized CPO by biometric magnetic nanoparticles exhibited excellent reusability and enantioselectivity in asymmetric synthesis of modafinil. More than 82% of original conversion rate and 70% enantiomeric excess (ee) value were observed after being run eight times. These results revealed that this immobilization strategy might have great potential in the application of other glycosyl-modified enzymes.

Mussel-Inspired Magnetic Nanoflowers as an Effective Nanozyme and Antimicrobial Agent for Biosensing and Catalytic Reduction of Organic Dyes

“…The peaks at 1075 and 802 cm –1 were assigned to the Si–O–Si vibrations. , The peaks at around 1623 cm –1 in MNPs due to NH 2 vibration and N–H stretching were representative of the free amino group in MNPs. The absorption peak at 2926 cm –1 was attributed to the −CH 2 – (asymmetric stretching) group as a result of APTES surface modification . Furthermore, the strong characteristic bond of stretching and vibration P–O was observed at 990, 1047, and 1149 cm –1 in PDA–Cu NFs and affirmed the existence of the phosphate group in them.…”

Immobilization of Alcohol Dehydrogenase on Titania Nanoparticles To Enhance Enzyme Stability and Remove Substrate Inhibition in the Reaction of Formaldehyde to Methanol

“…Therefore, surface charge in enzyme immobilization is a key factor in the immobilization yield and determining the density of immobilized enzyme. − Actually, with no conformational changes observed after immobilization the enzyme retains the most initial activity, whereas adsorption of the enzyme onto a carrier is relatively weak and the enzyme easily detaches from the support under gentle conditions . However, covalent linkage between enzyme and support ensures the highest strength of the bonding and improves the stability of enzyme in different conditions. − One of the most widely used reagents in covalent enzyme immobilization is glutaraldehyde, which can be used as a linker between support and enzyme. Glutaraldehyde can react with different portions of the enzyme, mainly involving the primary amino groups of proteins, and forms imine bonds between the biomolecule and the support …”

Oxidoreductases as a versatile biocatalytic tool to tackle pollutants for clean environment – a review

“…Chloroperoxidase (CPO) (EC 1.11.1.10) is part of the family of reducing oxide enzymes that catalyze the chlorination of organic compounds (i.e., it combines inorganic chloride substrates with H 2 O 2 ) . 113 This versatile enzyme-containing heme at its active site secreted by the marine fungus of Caldariomyces fumago (Leptoxyphium fumago) is recognized as a versatile catalyst to its catalytic activities, which include sulfoxidation, epoxidation, peroxidation, hydroxylation, dismutation, oxidation, and halogenation of various organic compounds. 114,115 For example, in the halogenation process, the catalytic cycle occurs through the in situ generations of halogenating species, such as X − (Cl or Br), and/or the formation of the hypohalogenate intermediate (HOX); both act as electrophiles and then accept electrons, forming a bond with a nucleophile and, thus, aids the halogenation of metabolites through the release of water (Fig.…”