Partial Purification of Peroxidase From Iraqi Radish Roots.

abbas., Ayatadnan.; sabbah., Majeedarsheed.

doi:10.21474/ijar01/3058

Cited by 2 publications

(2 citation statements)

References 5 publications

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“…1 The therapeutic application of L-asparaginase is documented in various situations like Hodgkin disease, acute lymphoblastic leukemia, reticle sarcoma, myelocytic leukemia, lymphosarcoma, melanosarcoma and pancreatic carcinoma. 2,3 This enzyme also nds an application in food industry for reduction of formation of acrylamide in fried foods. 4 L-Asparaginase has been obtained and investigated from various plant and microbial sources as reviewed by many researchers.…”

Section: Introductionmentioning

confidence: 99%

Hemocompatible glutaminase freel-asparaginase from marine Bacillus tequilensis PV9W with anticancer potential modulating p53 expression

et al. 2016

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Section: Introductionmentioning

confidence: 99%

Hemocompatible glutaminase freel-asparaginase from marine Bacillus tequilensis PV9W with anticancer potential modulating p53 expression

et al. 2016

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“…35 In the present study various inexpensive buffers that were readily available commercially, such as sodium phosphate buffer, potassium phosphate buffer, sodium acetate buffer, Tris base buffer, and distilled water were selected for media screening. 36,37 The influence of the extraction media on protein concentration and enzyme activity is shown (Fig. 1).…”

Section: Selection Of Extraction Media For Obtaining Crude Enzyme Ext...mentioning

confidence: 99%

Simple and efficient method for the extraction, isolation, and purification of peroxidase enzyme from wheat bran

Kumar,

Vasishta,

Pawar

2024

Biofuels Bioprod Bioref

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Peroxidase is an industrially important enzyme with a broad range of applications. In this study, the extraction, isolation, and purification of peroxidase was conducted with wheat bran as a feedstock. Several commercially available buffers (K2HPO4, Na3PO4, CH3COONa, and Tris‐base) were explored for the extraction of peroxidase from wheat bran. Of the tested media, sodium acetate buffer gave an excellent performance and displayed maximum protein (0.44 mg mL−1) and enzyme activity (28 U mL−1). A process optimization study was also conducted to obtain the maximum protein concentration and enzyme activity. The intensified process provided 1.39 mg mL−1 protein concentration with 90 U mL−1 enzyme activity with specific enzyme activity of 135.8 U mg−1. Crude enzyme was purified using a three‐step process: (a) precipitation, (b) ultrafiltration, and (c) chromatographic purification. Commercially available strong and weak ion exchange resins, with different surface properties, were tested for purification. The weak anion exchange resin showed an excellent performance for maximum binding of peroxidase. Adsorption study investigated the best fit model of Freundlich isotherm with maximum binding capacity of 54 mg mL−1. Overall, purification provided peroxidase with a protein concentration of 1.24 mg mL−1 and 727.58 U mg −1 specific enzyme activity with purity increased by around ~6.6 fold. The reported process provides a simple and efficient method for the extraction and purification of peroxidase enzyme from wheat bran for its efficient valorization.

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Partial Purification of Peroxidase From Iraqi Radish Roots.

Cited by 2 publications

References 5 publications

Hemocompatible glutaminase freel-asparaginase from marine Bacillus tequilensis PV9W with anticancer potential modulating p53 expression

Hemocompatible glutaminase freel-asparaginase from marine Bacillus tequilensis PV9W with anticancer potential modulating p53 expression

Simple and efficient method for the extraction, isolation, and purification of peroxidase enzyme from wheat bran

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