Isolation of Serratia marcescens SR1 as a Source of Chitinase Having Potentiality of Using as a Biocontrol Agent

Parani, K.; Shetty, G. P.; Saha, B. P.

doi:10.1007/s12088-011-0065-x

Cited by 23 publications

(20 citation statements)

References 23 publications

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“…V2 (Nawani et al, 2002) and Beauvería bassíana (Suresh & Chandrasekaran, 1999) had the highest activities at pH 4.5, 3.0 and 9.2, respectively. The optimum temperature for activities of chitinases secreted by Serratia marcescens SRI K was 37°C (Parani et al, 2011). In the present study, L capsici YS1215 retained its highest activity in a broad range of pH and the optimal pH of purified chitinase secreted by L. capsici YS1215 was at 5, 6 and 8, similar to previous results (Wang & Chang, 1997).…”

Section: Discussionsupporting

confidence: 90%

Purification and properties of a Meloidogyne-antagonistic chitinase from Lysobacter capsici YS1215

Lee

Anees

Park

et al. 2014

Nematol

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The root-knot nematodes, Meloidogyne spp., cause serious diseases in various plants and their chemical control may lead to environmental problems. Therefore, alternative control measures against the phytopathogenic nematodes are being sought. One of the potential targets against Meloidogyne spp. may be the chitinolysis and degradation of nematode eggs. Therefore, in the present study, a chitinolytic and nematicidal strain of Lysobacter capsici YS1215 was isolated from an agricultural field in Korea. The aim of this study was to purify chitinase secreted by L. capsici YS1215 and investigate its nematicidal role against Meloidogyne incognita. The chitinase secreted by L. capsici YS1215 was purified by protein precipitation with 80% ammonium sulphate, anion-exchange chromatography with DEAE-cellulose and gel-filtration chromatography with Sephadex G-100. By chitinase-active staining of the purified enzyme, a single band was obtained with an estimated molecular mass of 43.6 kDa. The optimal pH and optimal temperature for the highest chitinase activity were 6.0 and 40°C, respectively. The purified chitinase degraded the chitin layer of the eggshells and significantly reduced hatch of second-stage juveniles. The activity of chitinase secreted by L. cap.úci YS1215 was not affected by CoCh, MnCl2, MgCl2, CUSO4, CaCl2 or EDTA. The purified enzyme could also hydrolyse swollen chitin, glycol chitin, glycol chitosan and chitin powder Thus, the role of chitinase secreted by L. capsici YS1215 against Meloidogyne spp. may be useful for further development of a biocontrol agent.

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Section: Discussionsupporting

confidence: 90%

Purification and properties of a Meloidogyne-antagonistic chitinase from Lysobacter capsici YS1215

Lee

Anees

Park

et al. 2014

Nematol

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“…Since fungal cell walls and insect exoskeletons contain chitin, a homopolymer of β-1,4-linked N-acetyl-Dglucosamine residues as a major structural component, chitinases have been reported for their potential as biopesticides for the control of the plant diseases caused by various phytopathogenic fungi (3,4) and insect pests (1,5). Chitin is degraded into disaccharides and larger oligomeric saccharides by the action of chitinases (EC 3.2.1.14) through hydrolysis of the β-(1,4)-linkages (6), and these enzymes have been divided into 2 separate families, GH18 and GH19, based on amino acid sequences and their catalytic mechanisms (4).…”

Section: Introductionmentioning

confidence: 99%

Characterization, antifungal activity, and cell immobilization of a chitinase from Serratia marcescens MO-1

Okay¹,

Özdal²,

Kurbanoğlu³

2013

Turk J Biol

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Chitinases have the potential to control many pathogen species, such as fungi containing chitin on their cell walls. In the present study, chitinase from novel isolate Serratia marcescens MO-1, isolated from Poecilimon tauricola (Orthoptera: Tettigoniidae) in Turkey, was investigated. The optimum pH and temperature for the chitinase activity were found to be pH 7.0 (36.6 U/mL) and 50 °C (37.1 U/mL), respectively. Moreover, the activity was still high in acidic (23.0 U/mL at pH 3.0) and basic (17.3 U/mL at pH 11.0) conditions as well as at lower (29.5 U/mL at 20 °C) and higher (28.7 U/mL at 80 °C) temperatures. The enzyme was highly thermotolerant, keeping 63.7% (23.5 U/mL) of its activity after incubation at 90 °C for 15 min. Antifungal activity of the chitinase against Alternaria citri, Fusarium oxysporum, Trichoderma harzianum, Aspergillus niger, and Rhizopus oryzae was determined. In addition, chitinase production by immobilized S. marcescens MO-1 cells was monitored over 10 days; the enzyme activity was found to be 36-41 U/mL during this period. Our results showed that the chitinase from S. marcescens MO-1 seems to be valuable in terms of its biotechnological applications; it can be produced using immobilized cells and can be used against fungal pathogens as an alternative to chemical pesticides.

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“…This conclusion was also reported in previous studies of other strains of Serratia sp. (Parani et al, 2011;Zarei et al, 2011) …”

Section: Effect Of Initial Phmentioning

confidence: 99%

Optimization, purification, and characterization of an extracellular antifungal protein from Serratia marcescens DT3 isolated from soil in Vietnam

Tuyen¹,

Nguyen²,

Nguyen³

et al. 2017

Turk J Biol

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Gram-negative Serratia marcescens is a potential biological control agent of fungal plant diseases in many tropical regions. Its antifungal activity is due to the production of prodigiosin, protease, chitinase, and other substances that act to weaken the fungal cell wall and cause lysis. In the following investigation, a novel extracellular protein with antifungal activity against Rhizoctonia solani and Fusarium oxysporum was optimally produced, purified, and characterized from a native Serratia marcescens DT3. Under optimal conditions (medium containing 1.25% peptone, 0.5% yeast extract; temperature of 28 °C; initial pH of 7; culture time of 28 h), the antifungal activity of the extracellular extract was increased by a factor of 1.6-2.9 in comparison with the initial condition. The purified protein had an apparent molecular mass of 55 kDa. Its antifungal activity was retained at 80 °C for 30 min and after having been treated with proteinase K (0.5-4 µg/mL). The results of protein identification using a MALDI-TOF/TOF mass spectrometer suggested that the purified protein is indeed a serine 3-dehydrogenase.

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Isolation of Serratia marcescens SR1 as a Source of Chitinase Having Potentiality of Using as a Biocontrol Agent

Cited by 23 publications

References 23 publications

Purification and properties of a Meloidogyne-antagonistic chitinase from Lysobacter capsici YS1215

Purification and properties of a Meloidogyne-antagonistic chitinase from Lysobacter capsici YS1215

Characterization, antifungal activity, and cell immobilization of a chitinase from Serratia marcescens MO-1

Optimization, purification, and characterization of an extracellular antifungal protein from Serratia marcescens DT3 isolated from soil in Vietnam

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