Chitinase from Leaves of Beta vulgaris and other Higher Plants

El-Sayed, T Sanaa; Salem, Mohammed; Shehata, Abeer N.; Jwanny, W Etidal

doi:10.3923/pjbs.2000.250.256

Cited by 4 publications

(1 citation statement)

References 24 publications

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“…Chitinases are proteins that catalyze the hydrolysis of β-1,4-linkages of N -acetyl- d -glucosamine polymer of chitin; a major component of the exoskeleton of insects, crustacean shells and cell wall of many fungi (Bishop et al 2000; El-Sayed et al 2000; Passarinho and de Vries 2002). Chitinases are present in many higher plant species, although higher plants themselves do not contain chitin, chitosan or chitin-like substrate (Boller et al 1983; Hirano et al 1988).…”

Section: Introductionmentioning

confidence: 99%

Characterization of inflorescence-predominant chitinase gene in Metroxylon sagu via differential display

Roslan

Anji

2011

3 Biotech

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Chitinase is an enzyme that catalyzes the degradation of chitin, commonly induced upon the attack of pathogens and other stresses. A cDNA (MsChi1) was isolated from Metroxylon sagu and expressed predominantly in the inflorescence tissue of M. sagu, suggesting its role in developmental processes. The chitinase cDNA was detected and isolated via differential display and rapid amplification of cDNA ends (RACE). Primers specific to M. saguchitinase were used as probes to amplify the 3′-end and 5′-end regions of chitinase cDNA. Transcript analysis showed that chitinase is expressed in inflorescence and meristem tissues but was not detected in the leaf tissue. Sequence analysis of amplified cDNA fragments of 3′-end and 5′-end regions indicated that the chitinase cDNA was successfully amplified. The M. saguchitinase cDNA isolated was approximately 1,143 bp long and corresponds to 312 predicted amino acids. Alignments of nucleotide and amino acid have grouped this chitinase to family 19 class I chitinase.

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Section: Introductionmentioning

confidence: 99%

Characterization of inflorescence-predominant chitinase gene in Metroxylon sagu via differential display

Roslan

Anji

2011

3 Biotech

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In Vitro Effect of Antifungal Fractions from the Plants Baccharis glutinosa and Jacquinia macrocarpa on Chitin and β‐1,3‐Glucan Hydrolysis of Maize Phytopathogenic Fungi and on the Fungal β‐1,3‐Glucanase and Chitinase Activities

Buitimea-Cantúa

Rosas‐Burgos

Cinco-Moroyoqui

et al. 2013

Journal of Food Safety

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Baccharis glutinosa and Jacquinia macrocarpa are medicinal plants whose antifungal activity has been observed on maize phytopathogenic fungi. However, the specific site where those compounds act has not been studied. The objective of this work was to evaluate the hydrolytic effect of antifungal fractions from B. glutinosa (BgF) and J. macrocarpa (JmF) on β-glucan and chitin isolated from Aspergillus flavus and Fusarium verticillioides, as well as their inhibition activity on the fungal hydrolases β-glucanase and chitinase. The antifungal fractions did not show β-1,3-glucanase activity, instead, they showed chitinase activity against polymeric extracts from fungi. None of the antifungal fractions inhibited the chitinase activity of the fungi. However, both BgF and JmF antifungal fractions inhibited fungal β-1,3-glucanase activity acting as competitive inhibitors. It is possible that the antifungal fractions inhibit the β-1,3-glucanase activity affecting β-1,3-glucan synthesis, causing the production of a defective cell wall. These defects in the cell wall may allow the antifungal fractions to hydrolyze chitin causing delay in fungal growth. PRACTICAL APPLICATIONSStudies have proved that plants are one of the major sources for drug discovery and development, because plant-derived drugs have been reported to be safe and with no side effects. B. glutinosa and J. macrocarpa are plants used in traditional medicine by native people of Mexico, and their antifungal activity has been observed against mycotoxigenic fungi commonly associated with maize and other cereal grains. Although the effect on hyphae and spores suggests the interaction between the antifungal fractions and the fungal cell walls, as far as we know, there are no studies designed to elucidate the mode of action and the specific site of the cell wall where those compounds act. The results obtained in the present study suggest the presence of chitinase activity and a β-1,3-glucanase inhibitor found together in the antifungal fractions, which makes them a potential valuable alternative to synthetic fungicides for protecting maize and other cereal grains from fungal contamination.

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Purification and Biochemical Characterization of a Pathogenesis Related Endochitinase Arachis hypogaea

Younas¹,

Saleem²,

Tariq³

et al. 2016

IJAB

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Plants protect themselves by producing phytoalexins and pathogenesis related (PR) proteins in response to different physical and biological stresses as well as against pathological attack. In the present study, chitinase, a PR protein, from peanut seeds was purified to homogeneity by ammonium sulfate precipitation, gel filtration chromatography on Sephadex G-75 column and ion exchange chromatography on Q-Sepharose column. Chitinase was identified as monomeric protein with molecular mass of 30 kDa by SDS-PAGE. Chitinase activity was also evaluated on chitin agar plates showing distinct zones. The optimum pH and temperature of purified chitinase activity were found to be 5.2 and 35°C, respectively. The enzyme was stable within broad pH range of 3.6 to 7.6 and up to 55°C temperature. Amongst the various substrates, acid swollen chitin was found to be the best substrate for chitinase when used at the concentration of 1% exhibiting its high specificity in catalyzing glycosidic bonds between N-acetylglucosamine residues. Chitinase activity of the purified enzyme was inhibited by Hg 2+ and Ag 2+ at 1 mM concentration and enhanced by Ca . The increase in the presence of 2-mercaptomethanol demonstrates the existence of sulfhydryl groups in enzyme active site. The enzyme exhibited a strong inhibitory action towards a variety of fungal species including Fusarium oxysporum, Trichoderma reesei, Aspergillus flavus and A. niger. Purified chitinase showed fungicidal properties against A. flavus on white bread and therefore, could be applied in bakery products to inhibit the formation and growth of fungal colonies.

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Chitinase from Leaves of Beta vulgaris and other Higher Plants

Cited by 4 publications

References 24 publications

Characterization of inflorescence-predominant chitinase gene in Metroxylon sagu via differential display

Characterization of inflorescence-predominant chitinase gene in Metroxylon sagu via differential display

In Vitro Effect of Antifungal Fractions from the Plants Baccharis glutinosa and Jacquinia macrocarpa on Chitin and β‐1,3‐Glucan Hydrolysis of Maize Phytopathogenic Fungi and on the Fungal β‐1,3‐Glucanase and Chitinase Activities

Purification and Biochemical Characterization of a Pathogenesis Related Endochitinase Arachis hypogaea

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