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

Li, Zuming; Bai, Zhihui; Zhang, Baoguo; Li, Baojv; Jin, Bo; Zhang, Michael; Lin, Francis; Zhang, Hongxun

doi:10.1007/s12010-012-9758-9

Cited by 25 publications

(11 citation statements)

References 31 publications

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“…Optimum pH of 8.0-8.5 have been reported from a number of microbial sources, viz., A. flavus, A. terricola, Bacillus clausii, Pythium splendens, P. oxalicum and Cystofilobasidium capitatum (Chen and Tseng 1998;Yadav and Shastri 2007;Nakagawa et al 2005;Yadav et al 2009Yadav et al , 2013Li et al 2012). Temperature optimum of the purified pectin lyase was determined to be 40°C, which is in the same range 40-60°C as reported in the literature for PNLs of Thermoascus aurantiacus, Aspergillus giganticus and Fusarium decemcellulare MTCC 2079 (Yadav et al 2014;Pedrolli and Carmona 2014;Martins et al 2002) but different from temperature optima of 35°C for PNL of Lasiodiplodia theobromae (Adejuwon and Olutiola 2007).…”

Section: Discussionmentioning

confidence: 99%

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

et al. 2017

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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.

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Section: Discussionmentioning

confidence: 99%

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

et al. 2017

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“…Inoculated plates were incubated at 37°C for 24-48 h for isolation and screening on the basis of different colony morphologies (diameter, shape, color, surface and spores). The genomic DNAs of the isolates were extracted, amplified and sequenced according to the methods described by Li et al (2012). The 16S rDNA sequence data of the isolates reported here have been submitted to GenBank nucleotide sequence databases with the accession numbers shown in Tables 2 and 3.…”

Section: Methodsmentioning

confidence: 99%

Cultivable bacterial diversity and amylase production in two typical light-flavor Daqus of Chinese spirits

Chen

Zhang

et al. 2015

Frontiers in Life Science

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Culture-dependent methods and molecular techniques were used to simultaneously investigate the cultivable bacterial diversity and amylase production in two typical light- lus amyloliquefaciens). All of the bacterial isolates from the Hongxing Daqu could produce extracellular α-amylase with a maximum yield of 25.3 U/ml by B. cereus H17, whereas B. licheniformis H55 could produce a maximum glucoamylase yield of 41.6 U/ml. Some of the bacterial isolates from the Niulanshan Daqu could also produce extracellular α-amylase and glucoamylase. The maximum yield of 27.6 U/ml α-amylase was achieved by B. subtilis N3, and the maximum yield of 58.1 U/ml glucoamylase was achieved by B. cereus N25. Bacillus licheniformis, B. subtilis and B. cereus were not only the dominant bacteria, but also possessed high α-amylase and glucoamylase activities, which may play very important roles during fermentation.

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“…PCR cycling was performed with an Applied Biosystems Gene Amp PCR system 2700. PCR amplification reaction conditions were as previously described (Li et al ., , ).…”

Section: Methodsmentioning

confidence: 99%

Cultivable bacterial diversity and amylase production in three typical Daqus of Chinese spirits

Bai

Wang

et al. 2013

Int J of Food Sci Tech

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SummaryBoth culture-dependent method and molecular technique were firstly used to simultaneously investigate the cultivable bacterial diversity and amylase production in three typical Daqus of Chinese spirits. The results showed that both cultivable bacterial diversity and amylase production were obviously different. The species of nine bacteria from Deshan, nine from Baisha and six from Wuling Daqus were identified. The total bacterial strains of 17, 15 and 14, and 9, 16 and 10 could produce a-amylase and glucoamylase, respectively, from the Daqus, and the enzyme yields were different. Bacillus licheniformis, Bacillus subtilis and Bacillus amyloliquefaciens not only were dominant bacteria in the Daqus, but also possessed high activities of a-amylase and glucoamylase. By comparison, Bacillus cereus and Bacillus oleronius were found to be another predominant bacterial species and good producers of a-amylase and glucoamylase in Deshan and Wuling Daqus, respectively.

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

Cited by 25 publications

References 31 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

Cultivable bacterial diversity and amylase production in two typical light-flavor Daqus of Chinese spirits

Cultivable bacterial diversity and amylase production in three typical Daqus of Chinese spirits

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