Purification and characterization of an alkaline pectin lyase from Aspergillus flavus

Yadav, Sangeeta; Yadav, Pramod Kumar; Yadav, Dinesh; Yadav, K. D. S.

doi:10.1016/j.procbio.2008.01.015

Cited by 64 publications

(61 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Similar value of temperature stability has been reported in the literature for PNL from Oidiodendron echinulatum MTCC 1356 (Yadav et al 2008) though this value was higher than PNL of Aspergillus giganticus (Pedrolli and Carmona 2014). The thermostability of the purified enzyme was enhanced when exposed to 10 mM concentration of CaCl 2 while 1 M NaCl decreases the thermal stability.…”

Section: Discussionsupporting

confidence: 86%

“…These results are in agreement with our previous observation that EDTA inhibits the activity of pectin lyase (Table 2) produced by F.oxysporum. Retting of Crotolaria juncea fiber in the absence of EDTA has earlier been reported for fungal pectin lyases, namely Aspergillus flavus MTCC 7589, Aspergillus terricola MTCC 7588, Penicillium citrinum MTCC 8897, Aspergillus flavus MTCC 10938, and Fusarium decemcellulare MTCC 2079 (Yadav et al 2008(Yadav et al , 2009a(Yadav et al , b, 2013(Yadav et al , 2014. In contrast, efficient retting in the presence of EDTA has also been reported in the literature (Yadav et al 2012;DE Henrikkson et al 1997).…”

Section: Discussionmentioning

confidence: 90%

See 1 more Smart Citation

Purification, characterization and retting of Crotolaria juncea fibres by an alkaline pectin lyase from Fusarium oxysporum MTCC 1755

et al. 2017

View full text Add to dashboard Cite

Using solid-state fermentation, production of an industrially important pectin lyase from a fungal strain Fusarium oxysporum MTCC 1755 was attempted, which was further subjected to purification and characterization. The enzyme was purified by three steps, namely ammonium sulfate fractionation, cation-exchange chromatography on CM cellulose followed by gel filtration chromatography using Sephadex G-100 column. A 16-fold purification with 31.2% yield and 3.2 U/mg specific activity was achieved. The optimum pH of the purified enzyme was 9.0 and stability ranged from pH 5.0-7.0 for 24 h. Optimum temperature of purified enzyme was found to be 40°C while temperature stability ranged from 10 to 50°C for 30 min. The K m and k cat of the enzyme was 1.75 mg/ml and 83.3 s -1 , respectively. The purified enzyme was found to be highly stimulated by Ca 2? ions while sugars like mannitol and sorbitol, and salts like NaCl and CaCl 2 enhanced the thermostability. The purified pectin lyase was found suitable for retting of Crotolaria juncea fiber.

show abstract

Section: Discussionsupporting

confidence: 86%

Section: Discussionmentioning

confidence: 90%

Purification, characterization and retting of Crotolaria juncea fibres by an alkaline pectin lyase from Fusarium oxysporum MTCC 1755

et al. 2017

View full text Add to dashboard Cite

show abstract

“…It has a great degree of methyl esterification, which plays an important role in the adhesion of adjacent cells [1,2]. Enzymes that hydrolyze pectic substances are known as pectinases.…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of Alkaline Pectin Lyase from a Newly Isolated Bacillus clausii and Its Application in Elicitation of Plant Disease Resistance

Bai

Zhang

et al. 2012

Appl Biochem Biotechnol

View full text Add to dashboard Cite

Alkaline pectin lyase (PNL) shows potential as a biological control agent against several plant diseases. We isolated and characterized a new Bacillus clausii strain that can produce 4,180 U/g of PNL using sugar beet pulp as a carbon source and inducer. The PNL was purified to apparent homogeneity using ultrafiltration, ammonium sulfate fractionation, DEAE Sepharose Fast Flow, and Sephadex G-75 gel filtration. The purified PNL was found to be a monomeric protein with a molecular weight of 35 kDa, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). It demonstrated optimal activity with K m of 0.87 mg/ml at pH 10.0 and 60°C. The enzyme is stable in the pH range of 8.0-10.0 and temperature ≤40°C. Ca 2+ was found to stimulate the enzymatic activity of the PNL by up to 410 %. Mass spectrometric results gave 38 % match coverage with pectate lyase from B. clausii KSM-K16 (gi|56961845). The PNL was found to elicit disease resistance in cucumber seedlings, suggesting that it may have applications in biocontrol and sustainable agriculture.

show abstract

“…Whereas maximum pectin lyase activity at pH 8.0 confirms the alkalophilic nature of pectin lyase partially purified. The optimum pH of the pectin lyase of the papaya pericarp CV solo 8 is identical to that of Aspergillus niger isolated from orange peel (Batool et al, 2013) and Aspergillus flavus (Yadav et al, 2008). On the other hand, it is lower than the optimum pH (pH9.5) of pectin lyase isolated from Bacillus subtilis BPLSY1 (Al Balaa et al, 2014).…”

Section: Characterization Of Polygalacturonase and Pectin Lyasementioning

confidence: 84%

Partial purification and Characterization of Two Pectinases (Polygalacturonase and Pectin lyase) from Papaya Pericarp (Carica papaya cv. solo 8)

Didier¹,

Hubert²,

Parfait³

et al. 2017

Int.J.Curr.Microbiol.App.Sci

View full text Add to dashboard Cite

Purification and characterization of an alkaline pectin lyase from Aspergillus flavus

Cited by 64 publications

References 26 publications

Purification, characterization and retting of Crotolaria juncea fibres by an alkaline pectin lyase from Fusarium oxysporum MTCC 1755

Purification, characterization and retting of Crotolaria juncea fibres by an alkaline pectin lyase from Fusarium oxysporum MTCC 1755

Purification and Characterization of Alkaline Pectin Lyase from a Newly Isolated Bacillus clausii and Its Application in Elicitation of Plant Disease Resistance

Partial purification and Characterization of Two Pectinases (Polygalacturonase and Pectin lyase) from Papaya Pericarp (Carica papaya cv. solo 8)

Contact Info

Product

Resources

About