Purification and characterization of catalase from sprouted black gram (Vigna mungo) seeds

Kandukuri, Sai Srikar; Noor, Ayesha; Ranjini, S. Shiva; Vijayalakshmi, M.A.

doi:10.1016/j.jchromb.2012.01.029

Cited by 26 publications

(21 citation statements)

References 33 publications

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“…Similar pH and temperature conditions have been reported for the maximum activity of catalase isolated from different species e.g. enzyme from goat liver exhibited an optimum pH 6.8 (Chatterjee et al, 1989), camel liver enzyme and the enzyme from black gram have shown highest catalysis rate at pH 7 (Kandukuri et al, 2012;AlBar, 2012), enzyme isolated from apple have exhibited an optimum pH 7.5 and that isolated from pig liver has an optimum pH 8 (Arabaci et al, 2013). The catalase from van apple has shown maximum activity at 50°C (Yoruk et al, 2005).…”

Section: Discussionsupporting

confidence: 69%

“…The catalase from van apple has shown maximum activity at 50°C (Yoruk et al, 2005). The K M value of river buffalo liver catalase (58mM) is lower than that from goat liver (110mM) and bovine liver (93mM) (Kandukuri et al, 2012;Arabaci et al, 2013) indicating its greater affinity towards hydrogen peroxide. Present study reveals the first report on the purification and properties of liver catalase from river buffalo which is an unexplored species for its proteins and related genes.…”

Section: Discussionmentioning

confidence: 93%

“…Catalase has proven as a possible agent to support the intracellular drug delivery (Siwale et al, 2009) a biosensor for the determination of alcohol (Hnaien et al, 2010), and can be used in an assay for the quantification of cholesterol (Robinet et al, 2010). The enzyme has been purified and characterized from a wide range of organisms like plants, such as tobacco, van apple, parsley and black gram (Garcia et al, 2000;Yoruk et al, 2005;Lokman et al, 2007;Kandukuri et al, 2012), liver of many mammals like goat (Chatterjee et al, 1989), dog (Nakamura et al, 2000), bovine (Prakash et al, 2002), and from bacteria (Zamocky et al, 2011). Most of the literature reports describe the purification of enzyme through selective ammonium sulphate precipitation and chromatographic techniques like gel-filtration chromatography (Goyal and Anjan, 2008), ion-exchange chromatography based on CM (carboxymethyl) Sephadex, DEAE (diethylaminoethyl) Sephadex or DEAE cellulose (Aydemir and Kuru, 2003;Bilal et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

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Purification and Properties of Liver Catalase from Water Buffalo (Bubalus bubalis)

Nadeem¹,

Khan²,

Murtaza³

et al. 2015

S. Asian J. Life Sci.

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| Catalase is ubiquitous enzyme which catalyses the breakdown of hydrogen peroxide (H 2 O 2 ). The aim of present study was to purify and characterize the liver catalase from Bubalus bubalis, which is an important domestic animal in South Asia. The enzyme was purified to electrophoretic homogeneity by selective acetone precipitations and anion-exchange chromatography based on DEAE-Sephadex Colum. Purified enzyme displayed specific activity of 35753 units per mg of protein with 30.5 % recovery and 123 fold purification. Optimum activity was measured at pH 7 and 30°C. The K M value of purified catalase was calculated as 58mM for H 2 O 2 . Gel-filtration chromatography experiments indicate that the purified enzyme was a tetramer with MW of about 240 kDa. There was no effect of 10 to 50mM EDTA on the activity of enzyme after incubation for 30 min at 4°C. Our study reveals the first report on the purification and properties of catalase from river buffalo which is an unexplored species for its proteins. The isolated enzyme with high yield and specific activity, offers an attractive alternate for the bovine and porcine enzymes used in clinical laboratories.

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Section: Discussionsupporting

confidence: 69%

Section: Discussionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Purification and Properties of Liver Catalase from Water Buffalo (Bubalus bubalis)

Nadeem¹,

Khan²,

Murtaza³

et al. 2015

S. Asian J. Life Sci.

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“…e typical catalase reaction is the rapidly degradation of two molecules of H 2 O 2 to water and molecular oxygen [11][12][13]. Catalase has been biochemically, genetically studied, puri�ed, and characterized from many plants such as black gram (Vignamungo) seeds [14], dill (Anethum graveolens) [15], van apple [16], parsley [17], Nicotiana tabacum [18], cotton [19], Pinus taeda [20], sun�ower [21], and pumpkin [22].…”

Section: Introductionmentioning

confidence: 99%

Catalytic Properties and Immobilization Studies of Catalase from Malva sylvestris L.

Arabacı

Usluoglu

2012

Journal of Chemistry

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Catalase was partially purified fromMalva sylvestrisL. and immobilized onto chitosan. Then, its catalytic properties were investigated. (NH4)2SO4precipitation and dialysis were performed in the extracted enzyme. Further purification was performed with sephadex G-200 column. Kinetic studies of the purified enzyme activity were measured and characterized. The inhibitory effects of KCN, NaN3, CuSO4, and EDTA onM. sylvestrisL. catalase activity were observed except NaCl. Furthermore,M. sylvestrisL. catalase was immobilized covalently with glutaraldehyde onto chitosan particles. The pH and temperature optima as well as the changes in the kinetics (Km, Vmax) of the immobilized and freeM. sylvestrisL. catalase were determined. The Km value for immobilized catalase (23.4 mM) was higher than that of free enzyme (17.6 mM). Optimum temperature was observed higher than that of the free enzyme. The optimum pH was the same for both free and immobilized catalases (pH 7.50). Immobilized catalase showed higher storage and thermal stabilities than free catalases. Free catalase lost all its activity within 60 days whereas immobilized catalase lost 45% of its activity during the same incubation period at 4°C. The remaining immobilized catalase activity was about 70% after 8 cycles of batch operations.

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“…It is considered as a principal antioxidant enzyme in black gram seed. [18] Fungal contamination is one of the most threating pathogens to crop plants that alone contribute to a 25% loss of food crops and stored food grains throughout the world. The consumption of these contaminated crops or food products adversely affects human health causing growth disorders, liver and kidney damage, skin diseases, cancer, and other mutations.…”

Section: Examples Of Isoflavonoids Referencementioning

confidence: 99%

A Review Bioactive Components of Vigna mungo

Dhumal

Chaudhari²,

Chavan

2019

J. Drug Delivery Ther.

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The bioactive compound is secondary plant metabolites eliciting pharmacological or toxicological effects in man and animals. Legumes are a valuable source of proteins and nutrients for the majority of the world population. Vigna mungo is one of the important legume crops extensively cultivated in India and other parts of the world. Pulses and legumes have been gaining interest because they are an excellent source of bioactive compounds. The objective of this present review is to compile all relevant information published regarding bioactive components from the Vigna mungo. Various bioactive components reported in Vigna mungo were found and it includes flavonoids, isoflavonoids, phytoestrogens, phenolic acids, enzymes, fibers, starches, trypsin inhibitors, phytic acid, lectins, saponins, tocopherols, fatty acids and proteins. This review clearly demonstrates that Vigna mungo is rich in bioactive components and these components are located in various organs of the plant.

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Purification and characterization of catalase from sprouted black gram (Vigna mungo) seeds

Cited by 26 publications

References 33 publications

Purification and Properties of Liver Catalase from Water Buffalo (Bubalus bubalis)

Purification and Properties of Liver Catalase from Water Buffalo (Bubalus bubalis)

Catalytic Properties and Immobilization Studies of Catalase from Malva sylvestris L.

A Review Bioactive Components of Vigna mungo

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