EC Number   |
Protein Variants |
Reference |
|---|
   1.11.1.10 | E183H |
the mutation is detrimental to the chlorination and dismutation activity of chloroperoxidase, activities are reduced by 85% and 50% of the wild-type activity. Epoxidation activity of the mutant enzyme is significantly enhanced, about 2.5fold |
659196 |
| 1.11.1.10 | more |
chloroperoxidase is successfully entrapped in multi polysaccharide magnetic supports, which are developed based on a multi polysaccharide shell. Leakage of the enzyme is observed with single-shell polysaccharide coating. High CPO reusability is measured with a polymeric double-shell magnetic microsupport. The magnetic cores contain iron oxide nanoparticles, the polymer diminishes the interaction between the magnetic cores themselves, can improve the colloidal stability of the support, and prevent any interaction with the environment that would affect both support properties and enzyme stability. Different magnetic micro-supports, based on polydopamine-coated iron oxide nanoparticles with a multi polysaccharide shell, are developed and evaluated. Method overview. CPO is successfully immobilized with an efficiency of entrapment between 92% and 100% in the case of supports with chitosan in the interior or outer shell respectively. A very good chemical stability of the support under reaction conditions is observed in the case of an interior shell of alginate and an outer coating of chitosan, together with an excellent reusability of the immobilized enzyme, that is recycled to catalyze up to 25 consecutive reaction cycles. Chlorination of monochlorodimedone to dichlorodimedone is used as model reaction for chloroperoxidase catalytic assay |
763940 |
| 1.11.1.10 | more |
development of an immobilization method for chloroperoxidase (CPO) via carbohydrate-binding lectin protein, concanavalin A (ConA). ConA is attached on the surface of silica-coated magnetic nanoparticles (MNPs) for effective recovery (ConA/Fe3O4-SiO2). CPO shows about 100% activity recovery after its immobilization on ConA functionalized MNPs. After storing for four weeks, the immobilized CPO still maintains 80% activity while only 46% of activity of free enzyme is retained. Immobilized CPO by biometric magnetic nanoparticles exhibits excellent reusability and enantioselectivity in asymmetric synthesis of modafinil. More than 82% of original conversion rate and 70% enantiomeric excess (ee) value are observed after being run eight times. Synthesis and characterization of the ConA-functionalized magnetic nanoparticles, overview. CPO is fixed in the surface of nanoparticles without steric limitation and exposed to medium as free CPO. The immobilization temperature has little effect on immobilization efficiency, but CPO lost its activity at high temperature (>40°C). Meanwhile, CPO has a high immobilization efficiency at acidic conditions, but its activity greatly decreases at pH 7.0. Maximum immobilization efficiency and relative activity for immobilized CPO is obtained at 20°C and pH 6.0. ConA can efficiently conserve the natural activity of original CPO during the immobilization |
764828 |
| 1.11.1.10 | more |
enhancement of the catalytic performance of chloroperoxidase by co-immobilization with glucose oxidase (GOx) on magnetic graphene oxide (MGO), the catalytic efficiency (kcat/Km) of CPO immobilized on either MGO or MGO-GOx is approximately 2.1 and 2.5times higher, respectively, compared to that of the free CPO. The superior catalytic enzymes chloroperoxidase and glucose oxidase are co-immobilized onto the surface of MGO, method development and evaluation, overview. Graphene oxide/iron oxide (MGO) composites functionalized with Fe3O4 nanoparticles, providing the magnetic property, are used. The magnetism of the composites allows easy separation of the enzyme for reuse while the unique surface property of the composites significantly enhances the catalytic performance of the enzyme. The catalytic efficiency of immobilized CPO is much higher than that of free CPO. Immobilized CPO can be effectively and conveniently recovered and is ready to reuse. Enzyme cascade helps to harness the power of enzymes requiring auxiliary proteins. MGO-GOx-CPO reaches its peak activity (95.2%) when temperature is maintained between 42°C and 50°C compared to the optimal temperature of 35°C for the free enzyme. MGO-GOx-CPO reuse shows a good recovery in the presence of an external magnetic field, with about 38.5% activity remaining after 6 cycles of applications |
764088 |
| 1.11.1.10 | more |
immobilization of chloroperoxidase, method development, detailed overview. Halloysite nanotube (HNT) is a natural bio-compatible and stable nanomaterial available in abundance at low-cost. HNT is modified by two strategies to make it suitable for supporting immobilization of chloroperoxidase (CPO). Firstly, Fe3O4- nanoparticles are deposited on HNT, so magnetic separation can be used instead of centrifugation. Secondly, the magnetic HNT is modified by 3-aminopropyltriethoxysilane (APTES), which can provide amine group on surface of HNT and meanwhile inhibit the agglomeration of magnetic HNT. Then, HNT-Fe3O4 -APTES is linked with branched polyethyleneimine (PEI) to provide more amino for binding with enzyme. The so-prepared resin (CPO-HNT-Fe3O4-APTES-PEI) shows enhanced enzyme loading, reusability, improved thermal stability, and tolerance to organic solvents than free CPO. The affinity and specificity of immobilized enzyme to substrate is increased, Michaelis-Menten kinetic analysis |
764306 |
| 1.11.1.10 | more |
upon chemical modifications such as modifications of Lys residues with maleic and phthalic anhydride, of carboxyl groups with carbodiimide and ethanolamine or ethylenediamine, crosslinking with DMS and periodate oxidation, the loss of both chlorinating and peroxidative activity is observed for all types of modification, within the range of 39.5 and 56.8% for the chlorinating activity, and 16.4 and 44.5% for peroxidative activity |
743705 |
