Proteolytic enzyme mediated antagonistic potential of Pseudomonas aeruginosa against Macrophomina phaseolina.

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dc.contributor.authorIllakkiam, Devaraj
dc.contributor.authorAnuj, Nishanth Lipton
dc.contributor.authorPonraj, Paramasivan
dc.contributor.authorShankar, Manoharan
dc.contributor.authorRajendhran, Jeyaprakash
dc.contributor.authorGunasekaran, Paramasamy
dc.date.accessioned2013-11-20T04:53:00Z
dc.date.available2013-11-20T04:53:00Z
dc.date.issued2013-11
dc.description.abstractA new antagonistic bacterial strain PGPR2 was isolated from the mungbean rhizosphere and documented for the production of hydrolytic enzymes with antifungal activity. Based on the phylogenetic analysis of the 16S rRNA gene sequence and phenotyping, this strain was identified as Pseudomonas aeruginosa. Maximum protease activity (235 U/mL) was obtained at 24 h of fermentation. The protease was purified to homogeneity in three steps: ammonium sulphate precipitation, anion exchange chromatography on DEAE- cellulose resin and gel filtration chromatography using P6 column. The purified enzyme had a molecular weight of ~33 kDa. The purified protease exhibited maximum activity at pH 6.0 and retained 80% of activity in a pH range of 5.0 - 9.0. Proteolytic activity was maximum in a temperature range of 40–70 °C. However, the enzyme was stable at 40 °C for 60 min. Among the metals tested, Mg2+ enhanced the protease activity. Internal amino acid sequence of the protease obtained by MALDI -ToF and subsequent Mascot database search showed maximum similarity to the HtpX protease of P. aeruginosa strain PA7. Thus, by virtue of its early production time, thermostability and effective antifungal ability, the protease purified and characterized from P. aeruginosa PGPR2 has several potential applications as fungicidal agents in agriculture.en_US
dc.identifier.citationIllakkiam Devaraj, Anuj Nishanth Lipton, Ponraj Paramasivan, Shankar Manoharan, Rajendhran Jeyaprakash, Gunasekaran Paramasamy. Proteolytic enzyme mediated antagonistic potential of Pseudomonas aeruginosa against Macrophomina phaseolina. Indian Journal of Experimental Biology. 2013 Nov; 51(11): 1024-1031.en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/149413
dc.language.isoenen_US
dc.source.urihttps://nopr.niscair.res.in/handle/123456789/23454en_US
dc.subjectMacrophomina phaseolinaen_US
dc.subjectPlant growth promoting rhizobacteriaen_US
dc.subjectProteaseen_US
dc.subjectPseudomonas aeruginosaen_US
dc.subjectRhizosphereen_US
dc.subject.meshAscomycota --drug effects
dc.subject.meshChromatography, Liquid
dc.subject.meshElectrophoresis, Polyacrylamide Gel
dc.subject.meshEnzyme Stability
dc.subject.meshPeptide Hydrolases --isolation & purification
dc.subject.meshPeptide Hydrolases --metabolism
dc.subject.meshPeptide Hydrolases --pharmacology
dc.subject.meshProteolysis
dc.subject.meshPseudomonas aeruginosa --enzymology
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
dc.titleProteolytic enzyme mediated antagonistic potential of Pseudomonas aeruginosa against Macrophomina phaseolina.en_US
dc.typeArticleen_US
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