Spring cabbage peroxidases – Potential tool in biocatalysis and bioelectrocatalysis

Belcarz, Anna; Ginalska, Grażyna; Kowalewska, Barbara; Kulesza, Paweł J.

doi:10.1016/j.phytochem.2007.08.018

Cited by 24 publications

(14 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Px-cat fraction showed almost equal activity at neutral pH (7.0) suggesting that Px-cat fraction was stable in neutral pH range [46]. Red cabbage (Brassica oleracea var.…”

Section: Effect Of Phmentioning

confidence: 99%

Characterization of Plant Peroxidases and Their Potential for Degradation of Dyes: a Review

Kalsoom

Bhatti

Asgher

2015

Appl Biochem Biotechnol

View full text Add to dashboard Cite

Peroxidases are ubiquitously found in all vascular plants and are promising biocatalysts for oxidization of wide range of aromatic substrates including various industrial dyes. Peroxidases can catalyze degradation of chemical structure of aromatic dyes either by precipitation or by opening the aromatic ring structure. Both soluble and immobilized peroxidases have been successfully used in batches as well as in continuous processes for the treatment of aromatic dyes present in industrial effluents. Plant peroxidases are stable catalysts that retain their activities over a broad range of pH and temperatures. The performance of an enzyme for degradation process depends upon the structure of dyes and the operational parameters like concentration of enzyme, H2O2 and dye, incubation time, pH, and temperature. Recalcitrant dyes can also be mineralized by plant peroxidases in the presence of redox mediators. Thus, plant peroxidases are easily available, inexpensive, and ecofriendly biocatalysts for the treatment of wastewaters containing a wide spectrum of textile and non-textile synthetic dyes. This article reviews the recent developments in isolation and characterization of plant peroxidases and their applications for bioremediation of synthetic dyes.

show abstract

“…Px-cat fraction showed almost equal activity at neutral pH (7.0) suggesting that Px-cat fraction was stable in neutral pH range [46]. Red cabbage (Brassica oleracea var.…”

Section: Effect Of Phmentioning

confidence: 99%

Characterization of Plant Peroxidases and Their Potential for Degradation of Dyes: a Review

Kalsoom

Bhatti

Asgher

2015

Appl Biochem Biotechnol

View full text Add to dashboard Cite

show abstract

“…The colloidal suspension of PyBA-modified MWCNT was produced according to the procedure described earlier [18][19][20][21] and deposited by dropping 1.5 mL onto the glassy carbon electrode (GCE). The MWCNT/PyBA-AOx system was obtained by dissolving 3.0 mg of alcohol oxidase (AOx) and 1.0 mg of albumin from bovine serum (BSA) in 25 mL 0.1 M phosphate buffer solution (PBS), pH = 7.0.…”

Section: Preparation Of the Mwcnt/pyba-aox Systemmentioning

confidence: 99%

Bioelectrocatalytic Activity of Immobilized Alcohol Oxidase on 4‐(pyrrole‐1‐yl) Benzoic Acid Modified Carbon Nanotubes

Kowalewska

Jakubow

2016

Electroanalysis

Self Cite

View full text Add to dashboard Cite

A novel bioelectrocatalytic system was prepared by immobilizing alcohol oxidase (AOx) onto multiwalled carbon nanotubes (MWCNT) modified with 4‐(pyrrole‐1‐yl) benzoic acid (PyBA). Functional carboxylic groups from PyBA create covalent amide linkages with amine groups from the enzyme molecule and provide an anchor for the effective immobilization of AOx improving the stability of the whole system. The immobilized enzyme displayed a pair of reversible redox peaks of flavin adenine dinucleotide (FAD) cofactor with the formal potential E0’=−0.451 V. The response showed a surface‐controlled electrode process with the heterogeneous electron transfer rate constant ks=2.7 s−1. Under aerobic conditions AOx(FADH2) can be oxidized to AOx(FAD) by oxygen, which then reacts with ethanol decreasing the cathodic response, which could be used for ethanol detection with a high sensitivity 13.1 μA mM−1 cm−2. The lack of bioactivity towards ethanol in anaerobic conditions suggests the presence of two types of AOx molecules in the system: active with oxygen maintaining the direct electron transfer feature and not active without a redox mediator, due to the deeply embedded FAD cofactor. The polarization curve showed that the electrooxidation current of ethanol appears at −410 mV and reaches 2.0 µA cm−1 at −300 mV. In this case, the bioactivity of AOx to ethanol can be observed offering promising solution for the development of mediatorless systems for application to biosensors and biofuel cells.

show abstract

“…At present, horse radish is used as the major source of commercially available peroxidase, however, the researchers still investigate for new peroxidases of elevated stability and properties suitable for different biotechnological, biomedical and other application, e.g., spring cabbage peroxidase was suggested as a potential tool in biocatalysis and bio-electro catalysis [3]. Peroxidases have possibilities for applications clinically, in diagnostic kits, antibody labeling, waste water treatment and in food and paper industries.…”

Section: Introductionmentioning

confidence: 99%

“…As peroxidase is produced by number of microorganisms and plants, plants source is used for commercial production. Naturally thermo stable peroxidases have been described and include peroxidase from leaves of royal palm tree [6], spring cabbage peroxidase [3].…”

Section: Introductionmentioning

confidence: 99%

Determination of Kinetics of Peroxidase Enzyme Isolated From Brassica oleracea

Kesavan¹,

Puri²,

Mohanty³

2018

Insights Enzyme Res

View full text Add to dashboard Cite

Peroxidases are extensively found in plants, microorganisms and animals and are resourceful biocatalysts with a wide number of applications in biomedicine as well as biotechnology. The enzyme peroxidase was isolated from the leaves of Brassica oleracea using 0.2 M phosphate buffer at pH 7.0. Different dilutions of this crude enzyme were then examined for peroxidase activity assay. The substrate 4-aminoantipyrine-phenol was used to determine peroxidase activity. The effect of enzyme concentration, substrate concentration as well as temperature and pH on enzyme activity was then determined. The kinetic constants K m and V max were also determined. Based on Lineweaver-Burk plot with substrate concentration in the range of 4.25 × 10 -4 M to 16.15 × 10 -4 M the K m was found to be 7.14 mM and V max was found to be 0.1 mole/min. The optimum temperature was 50°C and the optimum pH was 8.0 for the peroxidase enzyme. These optimum conditions were used to determine enzyme activities in the cabbage sample.

show abstract

Spring cabbage peroxidases – Potential tool in biocatalysis and bioelectrocatalysis

Cited by 24 publications

References 38 publications

Characterization of Plant Peroxidases and Their Potential for Degradation of Dyes: a Review

Characterization of Plant Peroxidases and Their Potential for Degradation of Dyes: a Review

Bioelectrocatalytic Activity of Immobilized Alcohol Oxidase on 4‐(pyrrole‐1‐yl) Benzoic Acid Modified Carbon Nanotubes

Determination of Kinetics of Peroxidase Enzyme Isolated From Brassica oleracea

Contact Info

Product

Resources

About