A comparative analysis of GH18 chitinases and their isoforms from Beauveria bassiana: An in-silico approach

Bhagwat, Prashant; Amobonye, Ayodeji; Singh, Suren

doi:10.1016/j.procbio.2020.10.012

Cited by 16 publications

(12 citation statements)

References 55 publications

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“…As entomopathogens, the life cycle of different B. bassiana strains are organized and adapted to their invertebrate hosts, while as endophytes, they maintain a symbiotic relationship with their plant hosts. In this regard, previous attention has been mostly focused on some specific enzymes produced by B. bassiana being key factors in the fungus’ entomopathogenicity, viz., the chitinases, lipases and proteases [ 6 , 7 , 8 ]. However, only recently, different strains of B. bassiana have been shown to produce some biomass-degrading enzymes, indicating their less elucidated environmental role as a saprophyte [ 4 ].…”

Section: Introductionmentioning

confidence: 99%

Beauveria bassiana Xylanase: Characterization and Wastepaper Deinking Potential of a Novel Glycosyl Hydrolase from an Endophytic Fungal Entomopathogen

Amobonye

Bhagwat

Singh

2021

JoF

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Beauveria bassiana is an entomopathogenic fungus widely used as a biopesticide for insect control; it has also been shown to exist as an endophyte, promoting plant growth in many instances. This study highlights an alternative potential of the fungus; in the production of an industrially important biocatalyst, xylanase. In this regard, Beauveria bassiana SAN01 xylanase was purified to homogeneity and subsequently characterized. The purified xylanase was found to have a specific activity of 324.2 Umg−1 and an estimated molecular mass of ~37 kDa. In addition, it demonstrated optimal activity at pH 6.0 and 45 °C while obeying Michaelis–Menton kinetics towards beechwood xylan with apparent Km, Vmax and kcat of 1.98 mgmL−1, 6.65 μM min−1 and 0.62 s−1 respectively. The enzyme activity was strongly inhibited by Ag2+ and Fe3+ while it was significantly enhanced by Co2+ and Mg2+. Furthermore, the xylanase was shown to effectively deink wastepaper at an optimal rate of 106.72% through its enzymatic disassociation of the fiber-ink bonds as demonstrated by scanning electron microscopy and infrared spectroscopy. This is the first study to demonstrate the biotechnological application of a homogeneously purified glycosyl hydrolase from B. bassiana.

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Section: Introductionmentioning

confidence: 99%

Beauveria bassiana Xylanase: Characterization and Wastepaper Deinking Potential of a Novel Glycosyl Hydrolase from an Endophytic Fungal Entomopathogen

Amobonye

Bhagwat

Singh

2021

JoF

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“…Sinha et al [7] has reported that chitinases also have different basic and acidic proteins with molecular weight ranges from 25-35 kDa. Furthermore, recent studies have revealed the molecular weight of chitinases ranged from 34.5 to 49.5 KDa with theoretical pI 4.81-7.94 showing acidic to slightly basic nature of chitinase genes [15,44]. In our study, the molecular weight of β-1,3-glucanase and chitinase proteins were found to be 35.4 kDa and 33.5 kDa, respectively while theoretical pI for β-1,3- PLOS ONE glucanase was slightly basic (i.e., 8.50) and pI for chitinase protein was slightly acidic (i.e., 6.89).…”

Section: Discussionmentioning

confidence: 99%

“…chitinase and β-1,3-glucanase proteins. The higher proportions of random coils and α-helices provide stability to the enzyme [15,45,46]. β-1,3-glucanase and chitinase proteins belong to hydrolase family which hydrolyzes the β-1,3 and β-1,4 glycosidic linkages present in β-glucans and chitin, respectively [11,12].…”

Section: Plos Onementioning

confidence: 99%

“…β-1,3-glucanase and chitinase proteins are reported as best soldiers against fungal pathogens. In addition to plants, β-1,3-glucanase and chitinase proteins produced by bacteria [14] and fungi [15] also show excellent antifungal activities.…”

Section: Introductionmentioning

confidence: 99%

“…In silico studies of both β-1,3-glucanase and chitinase proteins from bacteria, fungi and different plants have been reported [12,[15][16][17]. However, there is a lack of in silico characterization and molecular interactions of both β-1,3-glucanase and chitinase proteins from wheat and their respective ligands in literature.…”

Section: Introductionmentioning

confidence: 99%

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Phylogenetic analyses, protein modeling and active site prediction of two pathogenesis related (PR2 and PR3) genes from bread wheat

et al. 2021

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Wheat is a major staple food and has been extensively grown around the globe. Sessile nature of plants has exposed them to a lot of biotic and abiotic stresses including fungal pathogen attack. Puccinia graminis f.sp. tritici causes stem rust in the wheat crop and leads to 70% decrease in its production. Pathogenesis-related (PR) proteins provide plants with defense against different fungal pathogens as these proteins have antifungal activities. This study was designed to screen Pakistani wheat varieties for PR2 and PR3 proteins and their in silico characterization. PR2 and PR3 genes were screened and isolated by PCR amplification from wheat variety Chenab-70 and Frontana, respectively. The nucleotide sequences of PR2 and PR3 genes were deposited in GenBank with accession numbers MT303867 and MZ766118, respectively. Physicochemical properties, secondary and tertiary structure predictions, and molecular docking of protein sequences of PR2 and PR3 were performed using different bioinformatics tools and software. PR2 and PR3 genes were identified to encode β–1,3–glucanase and chitinase proteins, respectively. Molecular docking of both PR2 and PR3 proteins with beta-glucan and chitin (i.e. their respective ligands) showed crucial amino acid residues involved in molecular interactions. Conclusively, molecular docking analysis of β–1,3–glucanase and chitinase proteins revealed crucial amino acid residues which are involved in ligand binding and important interactions which might have important role in plant defense against fungal pathogens. Moreover, the active residues in the active sties of these proteins can be identified through mutational studies and resulting information might help understanding how these proteins are involved in plant defense mechanisms.

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Biochemistry, Pathogenesis, and Parasitism of Beauveria

Figueroa,

Ferreira,

Mamani

et al. 2024

Entomopathogenic Fungi

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A comparative analysis of GH18 chitinases and their isoforms from Beauveria bassiana: An in-silico approach

Cited by 16 publications

References 55 publications

Beauveria bassiana Xylanase: Characterization and Wastepaper Deinking Potential of a Novel Glycosyl Hydrolase from an Endophytic Fungal Entomopathogen

Beauveria bassiana Xylanase: Characterization and Wastepaper Deinking Potential of a Novel Glycosyl Hydrolase from an Endophytic Fungal Entomopathogen

Phylogenetic analyses, protein modeling and active site prediction of two pathogenesis related (PR2 and PR3) genes from bread wheat

Biochemistry, Pathogenesis, and Parasitism of Beauveria

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