Immobilization of horseradish peroxidase onto kaolin by glutaraldehyde method and its application in decolorization of anthraquinone dye

Sekuljica, Z Natasa; Prlainovic, Z Nevena; Mijalković, Jelena; Stefanović, Bojana; Grbavcic, Z Sanja; Mijin, Dušan Ž.; Knežević‐Jugović, Zorica

doi:10.2298/hemind150220028s

Cited by 13 publications

(8 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Oxidation was monitored by following the change in absorbance at 590 nm (Ultrospec 3300 pro, Amersham Bioscience). Using the following mathematical expression the oxidation percentage was calculated :

Oxidation (%) = true[(\frac{A_{0} - A_{t}}{A_{0}}) true] \times 100

where A 0 is the initial absorbance of untreated dye solutions (control) and A t is the absorbance of dye solutions after enzymatic treatment.…”

Section: Methodsmentioning

confidence: 99%

“…The main drawbacks of these methods are production of huge amounts of activated sludge, incomplete dye removal, and high costs . An efficient synthetic dyes oxidation is possible using HRP and hydrogen peroxide . The use of oxidoreductive enzymes has become increasingly important because of their ability to transform harmful molecules in to innocuous and ecologically acceptable products under mild reaction conditions (pH and temperature) .…”

Section: Introductionmentioning

confidence: 99%

“…Direct Black‐38 was removed in high percentage, 92.9%, using HRP encapsulated into phospholipid‐templated titania particles . HRP immobilized onto kaolin via adsorption decolorized 92% of Acid Violet 109 within 35 min . Different phenols were removed using HRP immobilized onto magnetic Fe 3 O 4 /graphene oxide nanocomposite, electrospun microfibrous membranes, magnetic beads, or alkylamine CPG beads .…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Removal of Anthraquinone Dye by Cross‐Linked Enzyme Aggregates From Fresh Horseradish Extract

Šekuljica

Prlainović

Jakovetić

et al. 2016

CLEAN Soil Air Water

View full text Add to dashboard Cite

Horseradish roots (Armoracia rusticana) fresh extract was the source of unpurified horseradish peroxidase (HRP) which was used for the immobilization in a form of cross-linked enzyme aggregates (CLEAs). Among three precipitants used, acetone appeared to be the best choice for the precipitation. Acetone with 2% of glutaraldehyde gave the recovery of 30.3% of the enzyme initial activity. Horseradish peroxidase immobilized in a form of cross-linked enzyme aggregates (HRP-CLEAs) showed remarkable efficiency in Acid Violet 109 (AV 109) oxidation. Under optimal conditions (pH 4, dye concentration 30 mg L À1 , hydrogen peroxide concentration 0.1 mM), 72.4 and 88.9% of dye was oxidized using HRP-CLEAs in a batch and packed bed reactor, respectively. Higher stability was apparent in the packed bed reactor compared to the batch reactor where the mechanical instability of aggregates under constant agitation has been proved. After seven consecutive cycles the retained activity was 60 and 20% in the recycled packed bed and batch reactor, respectively. The feasibility of HRP-CLEAs application in dye oxidation was confirmed by significant dye oxidation percentage and reduction of the toxicity in the samples collected after enzymatic treatment in the recycled packed bed reactor, using brine shrimp, Artemia salina.

show abstract

Oxidation (%) = true[(\frac{A_{0} - A_{t}}{A_{0}}) true] \times 100

where A 0 is the initial absorbance of untreated dye solutions (control) and A t is the absorbance of dye solutions after enzymatic treatment.…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Removal of Anthraquinone Dye by Cross‐Linked Enzyme Aggregates From Fresh Horseradish Extract

Šekuljica

Prlainović

Jakovetić

et al. 2016

CLEAN Soil Air Water

View full text Add to dashboard Cite

show abstract

“…The reason for lower AV 109 dye oxidation with the initial dye concentration increase is a result of the activity loose caused by the formation of inactive "dead-end" complex [7,11]. In addition, very often the reaction products accumulation on the enzyme surface cause the obstacles in a substrate transfer to the enzyme active center reducing the productivity of the process [39]. Maximum oxidation of AV 109 dye 90.5% catalyzed by free HRP at the initial dye concentration of 30 mg l -1 was achieved.…”

Section: Optimal Conditions For Av 109 Dye Oxidation With Hrp-cleas Imentioning

confidence: 99%

The oxidation of anthraquinone dye using HRP immobilized as a cross-linked enzyme aggregates

Sekuljica¹,

Prlainovic²,

Stefanović³

et al. 2016

Adv techn

Self Cite

View full text Add to dashboard Cite

Finding a sustainable and ecofriendly methods for recalcitrant synthetic dyes removal is a researchers` major challenge. A carrier-free technique for commercial HRP immobilization is a focus of the present study. The immobilized biocatalyst, HRP-CLEAs with 580 U g-1 of the activity was obtained under the following immobilization conditions: precipitation reagent 80% ammonium sulphate, cross-linking reagent 1% of glutaraldehyde and protein-fedder, bovine serum albumin (BSA) concentration 5 mg ml-1. The obtained HRP-CLEAs showed great affinity towards model anthraquinone dye, C. I. Acid Violet 109. 88.4% of the dye was oxidized under the reaction conditions: pH 4, dye concentration 40 mg l-1 , H 2 O 2 concentration 1 mM and 0.1 U of HRP-CLEAs. The possibility of the immobilized biocatalyst application in five and eight oxidation cycles of the dye and pyrogallol (retained activity ~ 80%), respectively, indicates that HRP-CLEAs is an efficient and environmentally friendly biocatalyst with great potential in aromatic compounds removal from wastewater. This paper is a continuation of our earlier research related to HRP from horseradish extract immobilization in the form of CLEAs and the application in the wastewater colored with a synthetic anthraquinone dye treatment.

show abstract

“…This method is also cost-effective, able to retain the natural enzymatic structure and properties, and causes less disruption on enzyme structure and properties compared to immobilization via chemical modifications (e.g. covalent bonding and cross-linking) [12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Comparative Study on Lipase Immobilized onto Organo-Cation Exchanged Kaolin and Metakaolin: Surface Properties and Catalytic Activity

Elgubbi

Othman

Harun

2021

Bull. Chem. React. Eng. Catal.

View full text Add to dashboard Cite

Clay mineral has received much attention to be used as biocatalysts as it is cheaper, easily available and environmentally friendly. However, the use of unmodified clay, in particular kaolin for enzyme immobilization showed unsuitability of this support due to its negative charge. In this study, the hydrophobic properties of kaolin and metakaolin (kaolin heated to 650 °C) were adjusted by the intercalation with benzyltriethylammonium chloride (BTEA-Cl), at concentrations 2.0 times the cation exchange capacities (CEC) of the clays. The supports were then used for immobilization of lipase from Candida rugosa (CRL). From the study, the highest percentage of lipase immobilization was achieved (70.14%), when organo-modified metakaolin (2.0 MK) was used. The supports as well as the immobilized biocatalysts were then characterized by X-ray diffraction, Fourier transform infrared spectroscopy, scanning electron microscopy, and nitrogen adsorption techniques. Comparisons of the efficiencies of immobilized with free CRL in the synthesis of nonyl hexanoate showed that immobilized CRL achieved enzymatic activities of between 5.24×10−3 to 3.63×10−3 mmol/min/mg, while free CRL achieved enzymatic activity of 3.27×10−3 mmol/min/mg after 5 h of reaction at 30 ℃. The immobilized CRLs also maintained 70.81% – 80.59% thermostabilities at 70 ℃ as compared to the free CRL (28.13%). CRL immobilized on 2.0 NK and 2.0 MK also maintained 38.54% and 62.56%, respectively, of the initial activities after 10 continuous cycles, showing the excellent stability and reusability of the immobilized lipases, suitable as substitute for expensive, hazardous catalysts used in industries. Copyright © 2021 by Authors, Published by BCREC Group. This is an open access article under the CC BY-SA License (https://creativecommons.org/licenses/by-sa/4.0).

show abstract

Immobilization of horseradish peroxidase onto kaolin by glutaraldehyde method and its application in decolorization of anthraquinone dye

Cited by 13 publications

References 25 publications

Removal of Anthraquinone Dye by Cross‐Linked Enzyme Aggregates From Fresh Horseradish Extract

Removal of Anthraquinone Dye by Cross‐Linked Enzyme Aggregates From Fresh Horseradish Extract

The oxidation of anthraquinone dye using HRP immobilized as a cross-linked enzyme aggregates

Comparative Study on Lipase Immobilized onto Organo-Cation Exchanged Kaolin and Metakaolin: Surface Properties and Catalytic Activity

Contact Info

Product

Resources

About