Isolation, partial characterization, and cloning of an extracellular chitinase from the entomopathogenic fungus Verticillium lecanii

Yu, Gang; Xie, L.Q.; Li, J.T.; Sun, Xiaowen; Zhang, H.; Du, Quanjie; Li, Q.Y.; Zhang, S.H.; Pan, Hongyu

doi:10.4238/2015.march.27.13

Cited by 14 publications

(6 citation statements)

References 32 publications

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“…Our resuls showed that chitinase PeChi68 showed various inhibitory activities against conidial germination depending on the species of fungus, in aggrement with previous findings showing that bacterial and fungal chitinases have various inhibitory activities against spore germination depending on the source of spores (Banani et al, 2015; Broadway et al, 1995; Di Maro et al, 2010; Frankowski et al, 2001; Harman et al, 1993; Kamensky et al, 2003; Yu et al, 2015). It has been reported that one chitinase produced by a yeast can completely inhibit conidial germination of Monilinia spp., a post-harvest pathogen causing of brown rot of stone fruits (Banani et al, 2015).…”

Section: Discussionsupporting

confidence: 87%

Purification and Characterization of a Major Extracellular Chitinase from a Biocontrol Bacterium, Paenibacillus elgii HOA73

Kim

Park

Hur

et al. 2017

The Plant Pathology Journal

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Chitinase-producing Paenibacillus elgii strain HOA73 has been used to control plant diseases. However, the antimicrobial activity of its extracellular chitinase has not been fully elucidated. The major extracellular chitinase gene (PeChi68) from strain HOA73 was cloned and expressed in Escherichia coli in this study. This gene had an open reading frame of 2,028 bp, encoding a protein of 675 amino acid residues containing a secretion signal peptide, a chitin-binding domain, two fibronectin type III domains, and a catalytic hydrolase domain. The chitinase (PeChi68) purified from recombinant E. coli exhibited a molecular mass of approximately 68 kDa on SDS-PAGE. Biochemical analysis indicated that optimum temperature for the actitvity of purified chitinase was 50ºC. However, it was inactivated with time when it was incubated at 40ºC and 50ºC. Its optimum activity was found at pH 7, although its activity was stable when incubated between pH 3 and pH 11. Heavy metals inhibited this chitinase. This purified chitinase completely inhibited spore germination of two Cladosporium isolates and partially inhibited germination of Botrytis cinerea spores. However, it had no effect on the spores of a Colletotricum isolate. These results indicate that the extracellular chitinase produced by P. elgii HOA73 might have function in limiting spore germination of certain fungal pathogens.

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Section: Discussionsupporting

confidence: 87%

Purification and Characterization of a Major Extracellular Chitinase from a Biocontrol Bacterium, Paenibacillus elgii HOA73

Kim

Park

Hur

et al. 2017

The Plant Pathology Journal

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“…Usually, EPFs particularly L. lecanii produces extracellular pathogenesis-related proteins or insecticidal metabolites such as cyclodepsipeptide (bassianolide), chitinases, etc. [14,32,33]. In our study, L. lecanii-derived proteins would most probably be chitinases corresponding to 44 and 33 kDa [33,34].…”

Section: Discussionmentioning

confidence: 51%

“…[14,32,33]. In our study, L. lecanii-derived proteins would most probably be chitinases corresponding to 44 and 33 kDa [33,34]. Compared to buffertreated control plants, cotton plants treated exogenously by the foliar application of L. lecanii protein exhibited considerable reduction of fecundity rate of B. tabaci.…”

Section: Discussionmentioning

confidence: 54%

Sub-Lethal Effects of Lecanicillium lecanii (Zimmermann)-Derived Partially Purified Protein and Its Potential Implication in Cotton (Gossypium hirsutum L.) Defense against Bemisia tabaci Gennadius (Aleyrodidae: Hemiptera)

et al. 2021

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Whiteflies, Bemisia tabaci Gennadius (Aleyrodidae: Hemiptera), are a polyphagous economically destructive pest of several solanaceous crops around the world. Many secondary metabolites are synthesized by different biotrophic and necrotrophic fungi which are capable of inducing systemic resistance in plants against various phytophagous pests. The present laboratory work demonstrated the anti-insect impact of a protein extracted and purified partially from an entomopathogenic fungus (EPF) Lecanicillium lecanii (Zimmermann) against B. tabaci. Three different concentrations (i.e., 7.43, 11.15, and 22.31 μg mL−1) of this protein were bioassayed to assess its effect on the fecundity rate of B. tabaci on cotton (Gossypium hirsutum L.) plants. Furthermore, the possible implication of this fungal protein in defense pathways of cotton plants was evaluated by determining the expression profiles of salicylic acid (SA) and jasmonic acid (JA) pathways related to major genes through reverse transcription qPCR (RT-qPCR). According to the results, all protein concentrations exerted a significant (F3, 252 = 62.51; p ≤ 0.001) and negative impact on the fecundity rate of B. tabaci females. At the highest protein concentration (22.31 μg mL−1), the minimum rate of fecundity (i.e., 2.46 eggs female−1day−1) of B. tabaci was noted on the seventh day, whereas fecundity rates for the other two protein concentrations (i.e., 11.15 and 7.43 μg mL−1) were, respectively, 3.06 and 3.90 eggs day−1 female−1. The maximum rate of fecundity (6.01 eggs female−1day−1) was recorded in untreated (control) treatments. In addition, the foliar application of L. lecanii derived protein significantly upregulated all SA linked genes (OPR3, PPO1 and COI1) and slightly triggered up the JA linked genes (LOX1, UBQ7 and AOS) in the cotton plants. These findings revealed that this L. lecanii extracted partially purified protein triggered systemic resistance against B. tabaci in the cotton plants, proposing its putative effectiveness as an innovative biological control technique against B. tabaci and other phloem-feeding hemipteran pests. Nevertheless, further investigations such as purification and molecular and functional characterization of this L. lecanii-derived partially purified protein are required.

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“…Fungal chitinases play key roles in nutrition, morphogenesis, autolysis, competition, defense, or parasitism. Mycoparasitic, nematophagous [ 48 ], and entomopathogenic fungi [ 9 , 31 , 49 ] have been reported to produce chitinolytic enzymes that contribute to their biocontrol potentials. The functions and biocontrol potential of chitinases are widely known and well-reviewed [ 50–52 ].…”

Section: Diversity Of Roles In Naturementioning

confidence: 99%

Chitinase: diversity, limitations, and trends in engineering for suitable applications

2018

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Chitinases catalyze the degradation of chitin, a ubiquitous polymer generated from the cell walls of fungi, shells of crustaceans, and cuticles of insects. They are gaining increasing attention in medicine, agriculture, food and drug industries, and environmental management. Their roles in the degradation of chitin for the production of industrially useful products and in the control of fungal pathogens and insect pests render them attractive for such purposes. However, chitinases have diverse sources, characteristics, and mechanisms of action that seem to restrain optimization procedures and render standardization techniques for enhanced practical applications complex. Hence, results of laboratory trials are not usually consistent with real-life applications. With the growing field of protein engineering, these complexities can be overcome by modifying or redesigning chitinases to enhance specific features required for specific applications. In this review, the variations in features and mechanisms of chitinases that limit their exploitation in biotechnological applications are compiled. Recent attempts to engineer chitinases for improved efficiency are also highlighted.

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Isolation, partial characterization, and cloning of an extracellular chitinase from the entomopathogenic fungus Verticillium lecanii

Cited by 14 publications

References 32 publications

Purification and Characterization of a Major Extracellular Chitinase from a Biocontrol Bacterium, Paenibacillus elgii HOA73

Purification and Characterization of a Major Extracellular Chitinase from a Biocontrol Bacterium, Paenibacillus elgii HOA73

Sub-Lethal Effects of Lecanicillium lecanii (Zimmermann)-Derived Partially Purified Protein and Its Potential Implication in Cotton (Gossypium hirsutum L.) Defense against Bemisia tabaci Gennadius (Aleyrodidae: Hemiptera)

Chitinase: diversity, limitations, and trends in engineering for suitable applications

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