Purification and characterisation of two acidic peroxidase isoforms from the sheaths of bamboo shoots

Hsu, Shou-Kuo; Chung, Yun‐Chin; Chang, Chung‐Ju; Sung, Hong Gun

doi:10.1111/j.1365-2621.2012.03044.x

Cited by 7 publications

(7 citation statements)

References 35 publications

(46 reference statements)

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“…Similarly, the peroxidase from avocado showed an optimum activity at pH 3.8 [51]. The two acidic peroxidase isoforms from the sheaths of bamboo shoots had same optimum pH of 4.5 [52]. The purified Cocos nucifera isoenzymes TCWP1 and TCWP2 exhibited their maximal activities at pH 4.5 and 5.0, respectively [53].…”

Section: Effect Of Phmentioning

confidence: 94%

“…Peroxidase from fresh-cut Z. latifolia was stable in the pH range 4.0-7.0 while retained only 2.21 % of the activity after 1 min at 60°C [56]. The two acidic peroxidase isoforms from the sheaths of bamboo shoots were stable between 30 and 60°C [52]. The purified C. nucifera isoenzymes TCWP1 and TCWP2 were stable up to 50°C for 1 h [53].…”

Section: Ph and Thermal Stabilitymentioning

confidence: 95%

“…However, the two fractions of peroxidase, anionic (Px-ani) and cationic (Px-cat), from spring cabbage heads were optimally active at same 40°C temperature [46]. The optimum temperatures for function of two acidic peroxidase isoforms from the sheaths of bamboo shoots were 55 and 45-55°C, respectively [52]. The purified C. nucifera isoenzymes TCWP1 and TCWP2 exhibited its maximal activity at 40°C [53].…”

Section: Effect Of Temperaturementioning

confidence: 97%

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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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Section: Effect Of Phmentioning

confidence: 94%

Section: Ph and Thermal Stabilitymentioning

confidence: 95%

Section: Effect Of Temperaturementioning

confidence: 97%

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

Kalsoom

Bhatti

Asgher

2015

Appl Biochem Biotechnol

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“…Additionally, peroxidases from other plant sources such as cauliflower, white radish, and turnip, have been used for the degradation of various organic compounds [16–19]. Besides this, peroxidases from bamboo shoots and lemon peel have also been used for degrading dyes [20, 21]. The addition of redox mediator (RM) to the system has shown to enhance the degradation process to produce less toxic substances [22–25].…”

Section: Introductionmentioning

confidence: 99%

LC-MSMS based screening of emerging pollutant degradation by different peroxidases

et al. 2019

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BackgroundThe presence of a wide range of bioactive organic pollutants in wastewater and municipal water sources is raising concerns about their potential effects on humans. Not surprisingly, various approaches are being explored that can efficiently degrade these persistent organic pollutants. Use of peroxidases has recently been recognized as a novel remediation approach that may have potential advantages over conventional degradation techniques. However, testing the abilities of different peroxidases to degrade diverse emerging pollutants is tedious and cumbersome.ResultsIn the present study, we present a rapid and robust approach to easily test the degradability of 21 different emerging pollutants by five different peroxidases (soybean peroxidase, chloroperoxidase, lactoperoxidase, manganese peroxidase, and horseradish peroxidase) using an LC-MSMS approach. Furthermore, this approach was also used to examine the role of a redox mediator in these enzymatic degradation assays. Our results show that some of the organic pollutants can be easily degraded by all five of the peroxidases tested, whereas others are only degraded by a specific peroxidase (or when a redox mediator was present) and there are some that are completely resistant to degradation by any of the peroxidases tested (even in the presence of a redox mediator). The degradation of furosemide and trimethoprim by soybean peroxidase and chloroperoxidase, respectively, was investigated in detail by examining the transformation products generated during their degradation. Some of the products generated during enzymatic breakdown of these pollutants have been previously reported by others, however, we report many new transformation products.ConclusionsLC-MSMS approaches, like the one described here, can be used to rapidly evaluate the potential of different peroxidases (and redox requirements) to be used as bioremediation agents. Our preliminary result shows peroxidases hold tremendous potential for being used in a final wastewater treatment step.

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“…42,52,53 Although less frequent, there are reports of peroxidase with a molecular weight above at 100 KDa and this is due they be constituted as homo-or hetero-dimeric, trimeric ou tetrameric proteins, such as those found in leucaena stem (200 KDa), 54 papaya fruit (~240 KDa) and bamboo shoots (111 KDa). 55,56 Thus, the high molecular weight found in PdPI and PdPII may suggest that this is multimeric enzymes but further studies are needed to confirm this speculation.…”

Section: 38mentioning

confidence: 97%

Partial Purification and Thermal Stability of Two Peroxidases from Pithecellobium dulce (Roxb.) Benth. Aril

et al. 2016

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Resumo: Duas formas de peroxidase (POX), denominadas PdPI e PdPII, foram parcialmente purificadas de arilos de Pithecellobium dulce, utilizando precipitação com sulfato de amônio e cromatografia de troca iônica. O zimograma das proteínas obtidas após precipitação com sulfato de amônio na faixa de 60 a 90% de saturação (fração F6090), mostrou duas bandas com atividade peroxidásica. Na coluna de celulose DE-52, a atividade peroxidásica foi detectada nos picos não adsorvido (PdPI) e adsorvido (PdPII) eluído com NaCl 0,2 mol L -1 , sugerindo que a PdPI (~114 KDa) e a PdPII (~77 KDa) são proteínas básicas e ácidas, respectivamente, sendo a PdPI estável a 80 ºC. Este é o primeiro relato de purificação parcial de POX obtida de arilos de P. dulce, indicando que esta espécie pode ser uma nova fonte de enzimas para utilização em biossensores e outras aplicações biotecnológicas. Palavras-chave:Enzimas; Atividade peroxidásica; P. dulce; Zimograma. AbstractTwo peroxidase (POX) forms, named PdPI and PdPII, were partially purified from the Pithecellobium dulce aril, using ammonium sulfate precipitation and anion exchange chromatography. Zymography of the proteins obtained after precipitation in the range of 60-90% ammonium sulfate (F6090 fraction) showed two bands with peroxidase activity. In DE-52 cellulose column, the peroxidase activity was detected in unadsorbed peak (PdPI) and adsorbed peak eluted with 0.2 mol L -1 NaCl (PdPII) suggesting that PdPI (~114 KDa) and PdPII (~77 KDa) are basic and acidic proteins, respectively, being PdPI stable at 80 ºC. This is the first report of partial purification of POX from P. dulce aril, indicating that this species may be a new source of enzymes for use in biosensors and other biotechnological applications.

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Purification and characterisation of two acidic peroxidase isoforms from the sheaths of bamboo shoots

Cited by 7 publications

References 35 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

LC-MSMS based screening of emerging pollutant degradation by different peroxidases

Partial Purification and Thermal Stability of Two Peroxidases from Pithecellobium dulce (Roxb.) Benth. Aril

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