Isolation and characterization of a chitinase gene from entomopathogenic fungus Verticillium lecanii

Zhu, Yanping; Pan, Junting; Qiu, Junzhi; Guan, Xiong

doi:10.1590/s1517-83822008000200022

Cited by 22 publications

(11 citation statements)

References 9 publications

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“…Chitinases are the enzymes capable of chitin hydrolysis to low molecular weight end products that are of great interest as a potential biological control agent (Huang and Chen 2004;Makino et al 2006;Wang et al 2006). So, chitinolytic bacteria have a great potential in controlling insects under selected conditions (Zhu et al 2008;Osman et al 2015). Termites like other insects bear chitin for polymerizing and strengthening their exoskeleton and other tissue/organs like trachea and gut epithelium (Merzendorfer and Zimoch 2003;Al-Sawalmih 2007).…”

Section: Introductionmentioning

confidence: 99%

Potential of bacterial chitinolytic, Stenotrophomonas maltophilia, in biological control of termites

Jabeen

Hussain

Manzoor

et al. 2018

Egypt J Biol Pest Control

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Termites are important pest of crops, trees, and household wooden installments. Two species Coptotermes heimi and Heterotermes indicola are the major species of termites that results in great economic loss in Asia including Pakistan. Chitinases have drawn interest because of their relevance as biological control of pests. The study was performed to screen chitinolytic bacteria from dead termites and to determine their chitinolytic activity in degrading chitin content of termites. Ten isolates were obtained forming clear zones on chitin-containing agar plates. One isolate (JF66) had the highest (3.3 mm) chitinolytic index. Based on sequence of 16S rRNA gene, the isolate was identified as Stenotrophomonas maltophilia with (99%) similarity under Accession number KC849451 (JF66), and DNA G + C content was found to be (54.17%). S. maltophilia (JF66) produces chitinases upto 1757.41 U/ ml at 30°C and pH 6.0 employing diammonium phosphate as a nitrogen source. Chitinase gene was also extracted and gets sequenced that confirmed its presence. Whole culture and different concentrations of crude enzyme of the isolate were tested on the chitin covering of termites. Mortalities showed that crude enzyme of isolate could degrade chitin of both species of the termites C. heimi and H. indicola. Chitinase produced by S. maltophilia had potential application as biocontrol agent for termites, but it is assumed that purification of chitinases may produce more prominent results.

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Section: Introductionmentioning

confidence: 99%

Potential of bacterial chitinolytic, Stenotrophomonas maltophilia, in biological control of termites

Jabeen

Hussain

Manzoor

et al. 2018

Egypt J Biol Pest Control

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“…Since chitin is the major component of most fungal cell walls, a principal role has been attributed to enzymes from the chitinolytic system (12). Enzymatic lysis of fungal cell walls through extracellular chitinases has been implicated as a mechanism of biocontrol by bacterial agents (24,63,64).…”

Section: Introductionmentioning

confidence: 99%

Characterization of a chitinase with antifungal activity from a native Serratia marcescens B4A

Zarei¹,

Aminzadeh²,

Zolgharnein³

et al. 2011

Braz. J. Microbiol.

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Chitinases have the ability of chitin digestion that constitutes a main compound of the cell wall in many of the phytopathogens such as fungi. In the following investigation, a novel chitinase with antifungal activity was characterized from a native Serratia marcescens B4A. Partially purified enzyme had an apparent molecular mass of 54 kDa. It indicated an optimum activity in pH 5 at 45ºC. Enzyme was stable in 55ºC for 20 min and at a pH range of 3-9 for 90 min at 25ºC. When the temperature was raised to 60ºC, it might affect the structure of enzymes lead to reduction of chitinase activity. Moreover, the Km and Vmax values for chitin were 8.3 mg/ml and 2.4 mmol/min, respectively. Additionally, the effect of some cations and chemical compounds were found to stimulate the chitinase activity. In addition, Iodoacetamide and Idoacetic acid did not inhibit enzyme activity, indicating that cysteine residues are not part of the catalytic site of chitinase. Finally, chitinase activity was further monitored by scanning electronic microscopy data in which progressive changes in chitin porosity appeared upon treatment with chitinase. This enzyme exhibited antifungal activity against Rhizoctonia solani, Bipolaris sp, Alternaria raphani, Alternaria brassicicola, revealing a potential application for the industry with potentially exploitable significance. Fungal chitin shows some special features, in particular with respect to chemical structure. Difference in chitinolytic ability must result from the subsite structure in the enzyme binding cleft. This implies that why the enzyme didn't have significant antifungal activity against other Fungi

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“…including S. antibioticus , S. griseus , S. plicatus , S. lividans, S. aureofaciens and S. halstedii (21, 9). Chitinase has received attention due to its use as a biocontrol agent (14, 25) and also for developing transgenic plants (3). They have been used in a biological research for the generation of fungal protoplasts to degrade the fungal cell wall and also for being employed in human health care such as making ophthalmic preparations with chitinases (4).…”

Section: Introductionmentioning

confidence: 99%

Chitinase Production by Streptomyces sp. ANU 6277

Kolla¹,

Vijayalakshmi²

2009

Braz. J. Microbiol.

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Chitinase production by a terrestrial Streptomyces sp. ANU 6277 was studied under sub-merged fermentation. Chitinase production started after 24 h of incubation and reached maximum levels after 60 h of cultivation. A high level of chitinase activity was observed in the culture medium with pH 6 at 35°C. Culture medium amended with 1% chitin was found to be suitable for maximum production of chitinase. An optimum concentration of colloidal chitin for chitinase production was determined. Studies on the influence of additional carbon and nitrogen sources on chitinase production revealed that starch and yeast extract served as good carbon and nitrogen sources to enhance chitinase yield. Chitinase was purified from crude enzyme extract by single step gel filtration by Sephadex G-100. Purified chitinase of the strain exhibited a distinct protein band near 45 kDa by means of SDS-PAGE.

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Isolation and characterization of a chitinase gene from entomopathogenic fungus Verticillium lecanii

Cited by 22 publications

References 9 publications

Potential of bacterial chitinolytic, Stenotrophomonas maltophilia, in biological control of termites

Potential of bacterial chitinolytic, Stenotrophomonas maltophilia, in biological control of termites

Characterization of a chitinase with antifungal activity from a native Serratia marcescens B4A

Chitinase Production by Streptomyces sp. ANU 6277

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