Purification and characterization of soluble peroxidase from oil palm (Elaeis guineensis Jacq.) leaf

Deepa, Sathyaseelan S.; Arumughan, C.

doi:10.1016/s0031-9422(02)00167-x

Cited by 68 publications

(78 citation statements)

References 24 publications

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“…The molecular weight of peroxidase was estimated about 45 kDa compared the standard protein marker. The similar results about molecular weight have been stated by different researches [15,16].…”

Section: Sds-page Analysis Of Partitioned Peroxidasesupporting

confidence: 85%

Three-Phase Partitioning of Peroxidase from Flowers of Citrus sinensis for Use in Diagnostic Kit

Uckaya¹,

Demir²

2018

Asian J. Chem.

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Section: Sds-page Analysis Of Partitioned Peroxidasesupporting

confidence: 85%

Three-Phase Partitioning of Peroxidase from Flowers of Citrus sinensis for Use in Diagnostic Kit

Uckaya¹,

Demir²

2018

Asian J. Chem.

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“…Purified peroxidases have been obtained from diverse plant sources (Deepa, Arumughan 2002), such as spring cabbage, soy bean and rice leaves (Ito et al 1991), tea (Kvaratskhelia et al 1997), okra (Yemenicioglu et al 1998), Ipomoea palmetto (Srinivas et al 1999) and Copaifera longsdorffi (Maciel et al 2007). However, less attention has been directed toward sources that are naturally widely available and regarded as unwanted in the environment.…”

Section: Introductionmentioning

confidence: 99%

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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“…The PO purification process presented a similar chromatographic profile to that encountered for PO from palm oil by Deepa and Arumughan, 19 which used three purification steps, the last step using the exclusion molecular chromatography with a Sephadex G-100 column. In study, after four purification steps, with the last step Sephadex-G-100, reached 17% of REC of PO from wheat flour.…”

Section: Exclusion Molecular Chromatographymentioning

confidence: 98%

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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Purification and characterization of soluble peroxidase from oil palm (Elaeis guineensis Jacq.) leaf

Cited by 68 publications

References 24 publications

Three-Phase Partitioning of Peroxidase from Flowers of Citrus sinensis for Use in Diagnostic Kit

Three-Phase Partitioning of Peroxidase from Flowers of Citrus sinensis for Use in Diagnostic Kit

Catalytic and kinetic properties of purified Eichhornia crassipes leaf peroxidase

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

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