Single-step purification of peroxidase by 4-aminobenzohydrazide from Turkish blackradish and Turnip roots

Kalın, Ramazan; Atasever, Ali; Özdemir, Haşan

doi:10.1016/j.foodchem.2013.10.125

Cited by 33 publications

(34 citation statements)

References 20 publications

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“…These values are consistent with previous studies, where PO was recovered from several sources with optimal temperature between 30 and 50 °C. 1,[20][21][22] For both forms of PO, the pH that presented the greatest enzymatic activity was 5, a value consistent with findings when purified from Streptomyces sp 23 and Leucaena leucocephala. 24 In the evaluation of pH, there weren't significant differences in reaction pH of the crude extract between 4.5 and 6 and of the pure extract between 5 and 6.…”

Section: Optimal Reaction Conditionssupporting

confidence: 85%

“…In studies referencing PO, the optimal pH value varied between 4 and 8.5, depending on the purification source. 1,22,26,27 Characterization of optimal enzymatic pH stability is important when concerned with commercial exploration and industrial application. 15 …”

Section: Determination Of the Kinetic Constantsmentioning

confidence: 99%

“…1 PO are used in clinical diagnoses, immunoassays, pharmaceuticals, food and chemical development, synthesis, degradation and organic compounds transformation, and the removal of industrial waste and peroxides in food. [2][3][4] The action of PO enzyme has also been related to the degradation of mycotoxin Deoxinivalenol (DON).…”

Section: Introductionmentioning

confidence: 99%

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Peroxidase from soybean meal: obtention, purification and application in reduction of deoxynivalenol levels

Feltrin¹,

Fontes²,

Gracia³

et al. 2017

Quim. Nova

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This study established the conditions for the extraction of the enzyme peroxidase (PO) from soybean meal (SBM). An experimental design methodology was carried out in order to evaluate the effects of stirring rate time, pH and extracting solvent volume on the enzyme extraction. By using 5 g SBM and 50 mL phosphate buffer 10 mmol L -1 pH 4.7, 60 min stirring rate at 100 rpm, an enzyme with specific activity of 100 U mg -1 for SBM was obtained. Two techniques of purification were tested and compared for purification of peroxidase from soybean meal: triphasic partition (TPP) and molecular exclusion chromatography. TPP showcased a greater efficiency with 50% recuperation and a purification factor of 13.6. Peroxidase in crude and pure forms was characterized for kinetics, thermodynamics and biochemistry. The parameter of thermal inactivation indicates high stability to exposure time and temperature increase, showing that enzyme activity is not altered by the presence of constituents of the reaction medium. Peroxidase in crude form represented a greater upkeep in activity, keeping 50% activity for 114 days at 0 °C. Peroxidase in pure form had greater affinity for substrate and reduced Deoxynivalenol levels by 80%, 20% more than the crude form.

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Section: Optimal Reaction Conditionssupporting

confidence: 85%

Section: Determination Of the Kinetic Constantsmentioning

confidence: 99%

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Peroxidase from soybean meal: obtention, purification and application in reduction of deoxynivalenol levels

Feltrin¹,

Fontes²,

Gracia³

et al. 2017

Quim. Nova

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“…I chose citrus fruits as organic structure for this study, owing to its wide catalytic activity, high sensitivity and substrate specificity. It has been widely used in many applications, including removal of phenols from polluted waters, organic synthesis, biosensor design, medical and microanalytical studies [36], [43][44][45].…”

Section: Resultsmentioning

confidence: 99%

Antimicrobial and catalytic activity of citrus fruits peels mediated nano-flowers

Demırbas

2020

J. Biol. Macromol.

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In this work, plant extract-metal ions hybrid nanoflowers (HNFs) were synthesized and their catalytic and antimicrobial properties were examined. While the sweet and sour lemon peel extract (acquired in boil water) and its primary elements were engaged as organic elements in the creation of NFs, copper (II) ions (Cu 2+) were the inorganic element. Scanning Electron Microscopy (SEM), Energy-Dispersive X-ray (EDX) spectroscopy, and Fourier Transform Infrared Spectrometry (FT-IR) were examined to characterize the structures of the NFs. The structural examination showed that the existence of Cu-O and Cu-N bonds in NFs can be a sign of the creation of NFs. Antimicrobial activities of the NFs were systematically studied against Candida albicans (ATCC 90028), Staphylococcus aureus (ATCC 25923), and Escherichia coli (ATCC 25922) with broth microdilution and short time-kill assay. The peroxidasemimicking activity based on the NFs' Fenton-like response mechanism was assessed against guaiacol in the presence of H2O2. The findings have shown that plant extract-based hybrid NFs technology is promising and can find prospective applications in numerous technical areas.

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“…Peroxidases are frequently used in the studies of metabolic reactions, enzymatic functions, protein structures [15] and in clinical diagnoses, microanalytic applications, and the food and drug industry [16,17]. Mammalian POD enzymes are localized in milk, saliva, and tears as lactoperoxidases (LPO) [18] and in leukocytes and platelets as myeloperoxidases [6].…”

Section: Peroxidasesmentioning

confidence: 99%

An Important Milk Enzyme: Lactoperoxidase

Köksal¹,

Gülçın²,

Özdemir³

2016

Milk Proteins - From Structure to Biological Properties and Health Aspects

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It has been acknowledged since ancient times that milk and dairy products have a vital role in nutrition and contribute considerably to human health. Because of its content, Because of its content, it has many important effects on the life that include immunoglobulins, enzymes, hormones, growth factors, antibacterial agents, fat acids, vitamins, and minerals. Approximately indigenous enzymes have been reported in normal bovine milk, including lactoperoxidase. Lactoperoxidase LPO is a natural constituent of milk, saliva, and tears. It also exists in all mammary milk. LPO is an iron heme group basic glycoprotein, with a molecular weight of approximately kDa. The LPO enzyme catalyzes the H O +SCN -→ OSCN -+ H O reaction. Hydrogen peroxide and hypothiocyanate are indispensable for antimicrobial activity. The biological significance of LPO is involved in the natural host defense system against pathogenic microorganisms.

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Single-step purification of peroxidase by 4-aminobenzohydrazide from Turkish blackradish and Turnip roots

Cited by 33 publications

References 20 publications

Peroxidase from soybean meal: obtention, purification and application in reduction of deoxynivalenol levels

Peroxidase from soybean meal: obtention, purification and application in reduction of deoxynivalenol levels

Antimicrobial and catalytic activity of citrus fruits peels mediated nano-flowers

An Important Milk Enzyme: Lactoperoxidase

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