Partial purification and characterization of chitinase produced by Bacillus licheniformis B307

Akeed, Y.; Atrash, Faiza; Naffaa, Walid

doi:10.1016/j.heliyon.2020.e03858

Cited by 47 publications

(32 citation statements)

References 36 publications

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“…Compared to Gram-positive bacteria, 90% of the diversity of Gram-negative bacteria in marine ecosystems has traits that enhance survival of these organisms in extreme temperature, tolerance and rapid adaptation to nutrient deficiencies, and high salt concentration [ 33 , 34 ]. The chitinase activity of the mutated strains of UV-11 and EMS-13 showed values greater than earlier reports [ 27 ] with a maximum specific enzymatic activity of 14.2 U/mL in a strain of Bacillus licheniformis B307. On the other hand, our wild strain of Bacillus licheniformis SSCL-10 showed chitinolytic activity values of 3.4 U/mL, which is lower than the mutant values compared in this study and reported in our earlier studies [ 7 ].…”

Section: Discussioncontrasting

confidence: 77%

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Identification and Characterization of a Newly Isolated Chitinase-Producing Strain Bacillus licheniformis SSCL-10 for Chitin Degradation

Sasi

Duraipandiyan

Kannan³

et al. 2020

Archaea

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Chitinases or chitinolytic enzymes have different applications in the field of medicine, agriculture, and industry. The present study is aimed at developing an effective hyperchitinase-producing mutant strain of novel Bacillus licheniformis. A simple and rapid methodology was used for screening potential chitinolytic microbiota by chemical mutagenesis with ethylmethane sulfonate and irradiation with UV. There were 16 mutant strains exhibiting chitinase activity. Out of the chitinase-producing strains, the strain with maximum chitinase activity was selected, the protein was partially purified by SDS-PAGE, and the strain was identified as Bacillus licheniformis (SSCL-10) with the highest specific activity of 3.4 U/mL. The induced mutation model has been successfully implemented in the mutant EMS-13 (20.2 U/mL) that produces 5-6-fold higher yield of chitinase, whereas the mutant UV-11 (13.3 U/mL) has 3-4-fold greater chitinase activity compared to the wild strain. The partially purified chitinase has a molecular weight of 66 kDa. The wild strain (SSCL-10) was identified as Bacillus licheniformis using 16S rRNA sequence analysis. This study explores the potential applications of hyperchitinase-producing bacteria in recycling and processing chitin wastes from crustaceans and shrimp, thereby adding value to the crustacean industry.

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Section: Discussioncontrasting

confidence: 77%

“…The crude enzyme was partially purified from the culture supernatant (wild, UV mutant, and EMS mutant strains) using 65% saturated ammonium sulfate (SAS) precipitation at 4°C in stirring according to the method of Akeed et al [ 27 ]. Precipitation was done by centrifuging at 11,500 x g for 10 min at 4°C.…”

Section: Methodsmentioning

confidence: 99%

Identification and Characterization of a Newly Isolated Chitinase-Producing Strain Bacillus licheniformis SSCL-10 for Chitin Degradation

Sasi

Duraipandiyan

Kannan³

et al. 2020

Archaea

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“…For example, the expression of chitinases from Serratia marcescens PRNK-1 [ 18 ], Pedobacter sp. PR-M6 [ 19 ], and Bacillus licheniformis B307 [ 20 ] were incubated in 0.5% (w/v) colloidal chitin. Chitinases from Acremonium sp.…”

Section: Resultsmentioning

confidence: 99%

A Broad-Specificity Chitinase from Penicillium oxalicum k10 Exhibits Antifungal Activity and Biodegradation Properties of Chitin

Yan

Peng

et al. 2021

Marine Drugs

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Penicillium oxalicum k10 isolated from soil revealed the hydrolyzing ability of shrimp chitin and antifungal activity against Sclerotinia sclerotiorum. The k10 chitinase was produced from a powder chitin-containing medium and purified by ammonium sulfate precipitation and column chromatography. The purified chitinase showed maximal activity toward colloidal chitin at pH 5 and 40 °C. The enzymatic activity was enhanced by potassium and zinc, and it was inhibited by silver, iron, and copper. The chitinase could convert colloidal chitin to N-acetylglucosamine (GlcNAc), (GlcNAc)2, and (GlcNAc)3, showing that this enzyme had endocleavage and exocleavage activities. In addition, the chitinase prevented the mycelial growth of the phytopathogenic fungi S. sclerotiorum and Mucor circinelloides. These results indicate that k10 is a potential candidate for producing chitinase that could be useful for generating chitooligosaccharides from chitinous waste and functions as a fungicide.

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“…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%

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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Partial purification and characterization of chitinase produced by Bacillus licheniformis B307

Cited by 47 publications

References 36 publications

Identification and Characterization of a Newly Isolated Chitinase-Producing Strain Bacillus licheniformis SSCL-10 for Chitin Degradation

Identification and Characterization of a Newly Isolated Chitinase-Producing Strain Bacillus licheniformis SSCL-10 for Chitin Degradation

A Broad-Specificity Chitinase from Penicillium oxalicum k10 Exhibits Antifungal Activity and Biodegradation Properties of Chitin

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

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