Purification and Thermal Characterization of a Novel Peroxidase from a Local Chick Pea Cultivar

Bhatti, Haq Nawaz; Najma, A.; Asgher, Muhammad; Hanif, Muhammad Asif; Zia, Muhammad Anjum

doi:10.2174/092986606777841271

Cited by 18 publications

(16 citation statements)

References 26 publications

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“…Various studies have shown that peroxidase activity is susceptible to modulation by certain metal ions (Marzouki et al 2005;Bhatti et al 2006). The mixed type inhibition pattern obtained for each of the inhibitors indicates that they are able to inhibit E. crassipes leaf peroxidase by binding to either the free enzyme or its enzyme-substrate complex.…”

Section: Properties Of Purified Eichhornia Crassipes Leaf Peroxidasementioning

confidence: 94%

“…Other studies have shown peroxidase activity to have a similar optimum temperature range. Bhatti et al (2006) showed that activity of peroxidase from lettuce stem had an optimum temperature of 45 °C, while activity of peroxidase from cauliflower had optimum temperature of 30 °C (Koksal, Gulcin 2008).…”

Section: Properties Of Purified Eichhornia Crassipes Leaf Peroxidasementioning

confidence: 99%

See 1 more Smart Citation

Catalytic and kinetic properties of purified Eichhornia crassipes leaf peroxidase

Arise¹,

Osundahunsi²,

Farohunbi³

et al. 2016

EEB

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Peroxidase from Eichhornia crassipes leaf was purified 23.58 fold with 18.58% yield by means of (NH 4 ) 2 SO 4 precipitation, ion exchange and Sephadex G-75 gel filtration chromatography. Optimum temperature and substrate-dependent pH optimum for enzyme activity were 40 °C and pH 4.0, 9.0 and 6.0 for 2,2'-azino-bis-(3-ethylbenzthiazolin)-6-sulfonate (ABTS), guaiacol and pyrogallol, respectively. The enzyme had high pH stability and moderate thermal stability at temperatures up to 60 °C; the activation energy of inactivation of the enzyme was ~122.29 kJ mol -1 . Temperature-denaturing and spontaneous recovery were shown to be time-dependent while Ca 2+ -enhanced recovery of the denatured enzyme was in a time-dependent manner. The enzyme showed preferential affinity for ABTS over guaiacol and pyrogallol with K M values of 31.11, 21.91 and 6.45 mM respectively. It was reversibly inhibited by Pb 2+ , Hg 2+ and EDTA while urea only caused loss of ~30.40% activity after 60 min of incubation. E. crassipes leaf peroxidase has potential use for broad range of applications.

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Section: Properties Of Purified Eichhornia Crassipes Leaf Peroxidasementioning

confidence: 94%

Section: Properties Of Purified Eichhornia Crassipes Leaf Peroxidasementioning

confidence: 99%

Catalytic and kinetic properties of purified Eichhornia crassipes leaf peroxidase

Arise¹,

Osundahunsi²,

Farohunbi³

et al. 2016

EEB

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“…Similarly, peroxidase from peels of Citrus reticulata var. showed maximum activity at pH 6.0 [44] and the peroxidase from a local chick pea cultivar showed maximum activity at pH 5.5 [45].…”

Section: Effect Of Phmentioning

confidence: 99%

“…The peroxidase from a local chick pea cultivar showed maximum activity at 45°C [45]. Red cabbage (B. oleracea) showed a maximum activity at 30°C [47].…”

Section: Effect Of Temperaturementioning

confidence: 99%

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

Kalsoom

Bhatti

Asgher

2015

Appl Biochem Biotechnol

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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.

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“…[31] For example, molecular weight of POD was 44 kDa for cauliflower, [18] 38 kDa for artichoke, [32] 50 kDa for windmill palm tree, and 39 kDa for chickpea cultivar. [33] POD could be monomer such as found in Chlorella vulgaris or homotetramer such as found in oil from palm leaf. [34] Characterization studies Optimum pH and pH stability pH is crucial since it determines the ionization state of amino acid side chain on the enzyme and substrate.…”

Section: Molecular Weight and Puritymentioning

confidence: 99%

Purification, characterization and selected inhibition properties of peroxidase from haricot bean (Phaseolus vulgaris L.)

Köktepe

Altın

Tohma

et al. 2017

International Journal of Food Properties

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In this study, a cationic soluble peroxidase (POD) was homogeneously purified and biochemically characterized. The enzyme purification involved the combination of (NH 4 ) 2 SO 4 precipitation, CM-Sephadex cation exchange, and gel filtration chromatography. The purity of the enzyme was examined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, and one single prominent band was obtained with a molecular weight of approximately 45 kDa. The thermal and pH stability showed that the enzyme was stable at pH 5.0 and at 40°C, respectively. The activity remained stable at pH 4.0 at least for 10 days. K m and V max values were calculated from Lineweaver-Burk graph for each substrate. POD exhibited K m values of 0.0154 and 0.065 mM for guaiacol and H 2 O 2 , respectively. The enzyme was highly inhibited by sodium azide. This study could enrich the literature regarding the properties of POD from haricot bean that could be applicable to biomedical analysis. ARTICLE HISTORY

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Purification and Thermal Characterization of a Novel Peroxidase from a Local Chick Pea Cultivar

Cited by 18 publications

References 26 publications

Catalytic and kinetic properties of purified Eichhornia crassipes leaf peroxidase

Catalytic and kinetic properties of purified Eichhornia crassipes leaf peroxidase

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

Purification, characterization and selected inhibition properties of peroxidase from haricot bean (Phaseolus vulgaris L.)

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