Heterologous Expression, Purification and Characterization of a Peroxidase Isolated from Lepidium draba

Fattahian, Yaser; Riahi‐Madvar, Ali; Mirzaee, Reza; Torkzadeh‐Mahani, Masoud; Asadikaram, Gholamreza

doi:10.1007/s10930-017-9741-y

Cited by 12 publications

(8 citation statements)

References 48 publications

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“…Before estimating each kinetic parameter for LiPs, the purities of isozymes were checked for each purified PcLiPs (Figure S7). The RZ value is the critical measure of heme content in peroxidase and represents the purity of enzymes . Because heme in LiP participates in oxidizing activity of the enzyme, the heme needs to be well located in it.…”

Section: Resultsmentioning

confidence: 99%

Recombinant Lignin Peroxidase with Superior Thermal Stability and Melanin Decolorization Efficiency in a Typical Human Skin-Mimicking Environment

et al. 2023

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Recently, the desire for a safe and effective method for skin whitening has been growing in the cosmetics industry. Commonly used tyrosinase-inhibiting chemical reagents exhibit side effects. Thus, recent studies have focused on performing melanin decolorization with enzymes as an alternative due to the low toxicity of enzymes and their ability to decolorize melanin selectively. Herein, 10 different isozymes were expressed as recombinant lignin peroxidases (LiPs) from Phanerochaete chrysosporium (PcLiPs), and PcLiP isozyme 4 (PcLiP04) was selected due to its high stability and activity at pH 5.5 and 37 °C, which is close to human skin conditions. In vitro melanin decolorization results indicated that PcLiP04 exhibited at least 2.9-fold higher efficiency than that of well-known lignin peroxidase (PcLiP01) in a typical human skin-mimicking environment. The interaction force between melanin films measured by a surface forces apparatus (SFA) revealed that the decolorization of melanin by PcLiP04 harbors a disrupted structure, possibly interrupting π−π stacking and/or hydrogen bonds. In addition, a 3D reconstructed human pigmented epidermis skin model showed a decrease in melanin area to 59.8% using PcLiP04, which suggests that PcLiP04 exhibits a strong potential for skin whitening.

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Section: Resultsmentioning

confidence: 99%

Recombinant Lignin Peroxidase with Superior Thermal Stability and Melanin Decolorization Efficiency in a Typical Human Skin-Mimicking Environment

et al. 2023

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“…In order to find the optimum value of pH, peroxidase activity was measured at various pH values from 3 to 10 at ambient temperature. The optimum temperature of the reaction was also determined by the measurement of the FEE and DEE activity during the reaction at different temperature ranges (10–85 °C) under the optimum pH 34 .…”

Section: Methodsmentioning

confidence: 99%

“…Under the obtained optimum conditions, the reaction between TMB and hydrogen peroxide was carried out in the presence of the peroxidase and different concentrations of the substrate (0.06–0.6 mM TMB) and 1 mM H 2 O 2 34 . The rate of the reaction at different conditions can be calculated by Michaels–Menten (M–M) equation.…”

Section: Methodsmentioning

confidence: 99%

Modeling and optimization of radish root extract drying as peroxidase source using spouted bed dryer

Hamedi

Afsahi

Riahi‐Madvar

et al. 2021

Sci Rep

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The main advantages of the dried enzymes are the lower cost of storage and longer time of preservation for industrial applications. In this study, the spouted bed dryer was utilized for drying the garden radish (Raphanus sativus L.) root extract as a cost-effective source of the peroxidase enzyme. The response surface methodology (RSM) was used to evaluate the individual and interactive effects of main parameters (the inlet air temperature (T) and the ratio of air flow rate to the minimum spouting air flow rate (Q)) on the residual enzyme activity (REA). The maximum REA of 38.7% was obtained at T = 50 °C and Q = 1.4. To investigate the drying effect on the catalytic activity, the optimum reaction conditions (pH and temperature), as well as kinetic parameters, were investigated for the fresh and dried enzyme extracts (FEE and DEE). The obtained results showed that the optimum pH of DEE was decreased by 12.3% compared to FEE, while the optimum temperature of DEE compared to FEE increased by a factor of 85.7%. Moreover, kinetic parameters, thermal-stability, and shelf life of the enzyme were considerably improved after drying by the spouted bed. Overall, the results confirmed that a spouted bed reactor can be used as a promising method for drying heat-sensitive materials such as peroxidase enzyme.

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“…In order to nd the optimum value of pH, peroxidase activity was measured at various pH values from 3 to 10 at ambient temperature. The optimum temperature of the reaction was also determined by measurement of the FEE and DEE activity during the reaction at different temperature ranges (10-85 °C) under the optimum pH 31 .…”

Section: The Catalytic Activity Of the Enzymementioning

confidence: 99%

“…Under the obtained optimum conditions, the reaction between TMB and hydrogen peroxide was carried out in the presence of the peroxidase and different concentrations of the substrate (0.06-0.6 mM TMB) and the 1 mM H 2 O 2 31 . The rate of the reaction at different conditions can be calculated by Michaels-Menten (M-M) equation.…”

Section: Kinetic Parameters Of the Enzymatic Reactionmentioning

confidence: 99%

A novel method for production of peroxidase enzyme from garden radish root source using a spouted bed reactor modeling and optimization approach

Hamedi

Afsahi

Riahi‐Madvar

2021

Preprint

Self Cite

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The main advantages of the dried enzymes are the lower cost of storage and longer time of preservation for industrial applications. In this study for the first time, the spouted bed reactors were utilized for drying the garden radish (Raphanus sativus L.) root extract as a cost-effective source of the peroxidase enzyme. The response surface methodology (RSM) was used to evaluate the individual and interactive effects of main parameters (the inlet air temperature (T) and the air flow rate (Q)) on the residual enzyme activity (REA). The maximum REA of 38.7% was obtained at the T= 50 °C and Q= 1.4. In order to investigate the drying effect on the catalytic activity, the optimum reaction conditions (pH and temperature), as well as kinetic parameters, were investigated for the fresh and dried enzyme extracts (FEE and DEE). The obtained results showed that optimum pH was decreased about 12.3% while 85.7% increase was observed in optimum temperature of DEE compare to FEE. Moreover, kinetic parameters, thermal-stability, and shelf life of the enzyme were considerably improved after drying by the spouted bed. Overall, the results confirmed that a spouted bed reactor can be used as a promising method for drying heat-sensitive materials such as peroxidase enzyme.

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Heterologous Expression, Purification and Characterization of a Peroxidase Isolated from Lepidium draba

Cited by 12 publications

References 48 publications

Recombinant Lignin Peroxidase with Superior Thermal Stability and Melanin Decolorization Efficiency in a Typical Human Skin-Mimicking Environment

Recombinant Lignin Peroxidase with Superior Thermal Stability and Melanin Decolorization Efficiency in a Typical Human Skin-Mimicking Environment

Modeling and optimization of radish root extract drying as peroxidase source using spouted bed dryer

A novel method for production of peroxidase enzyme from garden radish root source using a spouted bed reactor modeling and optimization approach

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