Production and activities of chitinases and hydrophobins from Lecanicillium lecanii

Rocha-Pino, Zaizy; Vigueras, Gabriel; Shirai, Kohji

doi:10.1007/s00449-011-0517-z

Cited by 24 publications

(20 citation statements)

References 24 publications

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“…Our chitinase belongs to Group II with MW of 32-33 kDa, and. according to Rocha-Pino et al (2011), it could be an exochitinase. The purification factor for chitinase from L. lecanii 43H was lower than those of M. anisopliae (4.98) and G. virens (105) and as high as that of chitinase from T. hariuzaum (1.3).…”

Section: Discussionmentioning

confidence: 99%

An extracellular antifungal chitinase from Lecanicillium lecanii: purification,properties, and application in biocontrol against plant pathogenic fungi

Nguyen¹,

Quyen²,

Nguyen³

et al. 2015

Turk J Biol

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IntroductionChitin, a homopolymer of N-acetyl glucosamine (GlcNAc) residues linked by β-1,4 bonds, is widely distributed in nature as a component of crustacean exoskeleton, insect outer shell, diatoms, fungal cell walls, and squid pens. It is the second most abundant biopolymer next to cellulose, as well as a constant source of renewable raw materials on earth (Tharanathan and Kittur, 2003). Two enzymes catalyzing hydrolysis of the chitin chain to its monomer by synergistic and consecutive action are endochitinases (EC 3.2.1.14), which randomly hydrolyze the β-1,4 glycosidic bonds of chitin, and N-acetylglucosaminidases (chitobiase, EC 3.2.1.30), which preferentially break lower chitooligomers to produce N-acetyl glucosamine (GlcNAc) monomers (Patil et al., 2002).Chitinases play important roles in biological activities such as nutrient intake, morphological change, defense, and attack. Fish and squid can digest chitinous substances as food by using chitinases in the stomach and liver (Matsumiya and Mochizuki, 1996;Matsumiya et al., 1998), whereas insects and shellfish use chitinases to degrade chitinous substances in the exoskeleton during ecdysis (Kramer and Koga, 1986). In plants, chitinases serve to attack fungal pathogens that contain chitinous substances for self-defense (Singh et al., 2007). Chitinases have received considerable attention due to potential applications in the biocontrol of plant pathogenic fungi and insects (Patil et al., 2002) as a target for biopesticides. Chitinases play an important role in the virulence of many bacteria and fungi for insects and fungi by lysing their cell walls. In addition, chitinases inhibit spore germination and germ tube elongation of the phytopathogenic fungi (Mathivanan et al., 1998). Chitinases can be used widely in the production of (GlcNAc)n and GlcNAc, the formation of yeast and fungal spheroplast and protoplast, and the bioconversion of chitin waste to single cell protein for animal feed (Mathivanan et al., 1998).Chitinases are produced by various microorganisms such as bacterial (Singh et al., 2008) and fungal antagonists of other fungal mycoparasistes, nematophagous and entomopathogenic fungi, and others (Rocha-Pino et al., 2011). Because of their wide range of biotechnological applications, chitinases have been purified and characterized.

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Section: Discussionmentioning

confidence: 99%

An extracellular antifungal chitinase from Lecanicillium lecanii: purification,properties, and application in biocontrol against plant pathogenic fungi

Nguyen¹,

Quyen²,

Nguyen³

et al. 2015

Turk J Biol

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“…Contact angle was calculated according to the eq. . Analyses were conducted by quadruplicate, in three different random locations on each surface.…”

Section: Methodsmentioning

confidence: 99%

Fibroblast viability and inhibitory activity against Pseudomonas aeruginosa in lactic acid–grafted chitosan hydrogels

Espadín

Vázquez

Tecante

et al. 2013

J of Applied Polymer Sci

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Chitosan (Ch) from biologically obtained chitin by lactic acid fermentation process was successfully grafted with lactic acid following three different procedures, direct d,l‐lactic acid attachment with and without the aid of p‐toluene sulfonic acid catalyst and by ring‐opening of l‐lactide. The produced materials behave as hydrogels responsive to pH changes and were characterized by X‐ray diffraction analyses, swelling behavior, erosion, contact angle, and thermally. In addition, mechanical studies in films of the synthetized materials demonstrate that the increase in grafting improved the mechanical properties in terms of tensile strengths. All the grafted Chs showed inhibition of the pathogenic bacteria Pseudomonas aeruginosa, which corroborate the preservation of antimicrobial activities in the modified Ch. The study on cell attachment and viability of fibroblasts onto the grafted Ch films evidenced that regardless of the low mechanical improvement in the lowest incorporation of lactic acid (31%), it rendered the materials with the highest adherence and viability of fibroblasts. Nonetheless, lactic acid incorporation enhanced cell viability in all synthetized materials as compared to native Ch. © 2013 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2014, 131, 40252.

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“…Fungal pathogenesis is a complex process that includes adherence, penetration, and digestion and requires the production of hydrolytic enzymes that penetrate the chitinous cell wall and cuticle, an extremely thick barrier preventing the entry of most fungal pathogens and insects (Li et al, 2004). Chitinases (EC 3.2.1.1.4) are major extracellular-degrading enzymes responsible for the random hydrolysis of internal links of the chitin chain to small-molecule nutrients, which are required during fungus penetration into the insect cuticle or fungal cell wall (Rocha-Pino et al, 2011). In addition, chitinases in plants are important enzymes of protective approaches targeting fungal pathogens, since chitinases in plants can degrade chitin in the fungi cell wall.…”

Section: Introductionmentioning

confidence: 99%

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

Xie

et al. 2015

Genet. Mol. Res.

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ABSTRACT. The entomopathogenic fungus Verticillium lecanii is a well-known biocontrol agent of fungal phytopathogens, as well as insect pests. A 42-kDa chitinase belonging to family 18 of the glycosyl hydrolases was isolated and partially characterized. Chitinase was purified using successive column chromatography on phenyl-sepharose, DEAE-sepharose, and CM-sepharose. The enzyme showed the highest activity at 40°C and pH 4.6. Enzyme activity was strongly activated in the presence of Mg 2+. The purified enzyme showed inhibitory activity of spore germination against several plant pathogens, particularly Fusarium moniliforme. The genomic DNA and cDNA sequences were resolved by polymerase chain reaction amplification and sequencing. Protein modeling and comparative investigation of different chitinase amino acids showed that chitinases are conserved in parasitic fungi.

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Production and activities of chitinases and hydrophobins from Lecanicillium lecanii

Cited by 24 publications

References 24 publications

An extracellular antifungal chitinase from Lecanicillium lecanii: purification,properties, and application in biocontrol against plant pathogenic fungi

An extracellular antifungal chitinase from Lecanicillium lecanii: purification,properties, and application in biocontrol against plant pathogenic fungi

Fibroblast viability and inhibitory activity against Pseudomonas aeruginosa in lactic acid–grafted chitosan hydrogels

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

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