First report of a bifunctional chitinase/lysozyme produced by Bacillus pumilus SG2

Ghasemi, Seyedhadi; Ahmadian, Gholamreza; Sadeghi, Mehdi; Zeigler, Daniel R.; Rahimian, Heshmatollah; Ghandili, Soheila; Naghibzadeh, N; Dehestani, Ali

doi:10.1016/j.enzmictec.2010.11.001

Cited by 32 publications

(27 citation statements)

References 22 publications

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“…Yan et al [21] have reported that Bacillus subtilis SL-13 chitinase enzyme has an optimum activity at 50°C, Vaidya et al [20] have reported that Alcaligenes xylosoxoxydans chitinase enzyme has an optimum activity at 50°C, Bhushan & Hoondal [22] have reported an optimum activity of Bacillus chitinase enzyme at 45-55°C, Ghasemi et al [23] have reported that ChiS chitinase enzyme by the bacterium Bacillus pumilus SG2 has an optimum activity at 50°C, and Zhang et al [19] have reported that Stenotrophomonas maltophilia C3 chitinase enzyme showed an optimum activity at 45-50°C. These results support the findings obtained in our study.…”

Section: Resultsmentioning

confidence: 99%

Purification of Chitinase enzymes from Bacillus subtilis bacteria TV-125, investigation of kinetic properties and antifungal activity against Fusarium culmorum

Senol

Nadaroğlu

Dikbaş

et al. 2014

Ann Clin Microbiol Antimicrob

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BackgroundChitin is the main structural component of cell walls of fungi, exoskeletons of insects and other arthropods and shells of crustaceans. Chitinase enzyme is capable of degrading chitin, and this enzyme can be used as a biological fungicide against phytopathogenic fungi, as well as an insecticide against insect pests.MethodsIn this study, 158 isolates, which were derived from bacteria cultures isolated from leaves and root rhizospheres of certain plants in Turkey, were selected after confirming that they are not phytopathogenic based on the hypersensitivity test performed on tobacco; and antifungal activity test was performed against Fusarium culmorum, which is a pathogenic fungi that cause decomposition of roots of vegetables. Accordingly, chitinase enzyme activity assay was performed on 31 isolates that have an antifungal activity, and among them the isolate of Bacillus subtilis TV-125 was selected, which has demonstrated the highest activity.ResultsChitinase enzyme was purified by using ammonium sulphate and DEAE-sephadex ion exchange chromatography. Ammonium sulphate precipitation of chitinase enzyme from Bacillus subtilis TV-125 isolate was performed at maximum range of 0-20%, and 28.4-fold purification was obtained with a 13.4% of yield. Optimum activity of the purified enzyme was observed at pH 4.0 and at 50°C of temperature. In addition, it was identified that Bacillus subtilis TV-125A isolate retains 42% of its activity at 80°C temperature.ConclusionIn the last phase of the study, chitinase enzyme purified from Bacillus subtilis TV-125A was tested on four fungal agents, although all the results were positive, it was particularly effective on F. culmorum according to the findings.

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Section: Resultsmentioning

confidence: 99%

Purification of Chitinase enzymes from Bacillus subtilis bacteria TV-125, investigation of kinetic properties and antifungal activity against Fusarium culmorum

Senol

Nadaroğlu

Dikbaş

et al. 2014

Ann Clin Microbiol Antimicrob

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“…Only a few studies on a Bacillus pumilus GH family 18 chitinase and two P. aeruginosa chitinases of unspecified GH family have, however, shown such hydrolytic activity (Ghasemi et al, 2011;Wang & Chang, 1997), whereas Enterococcus faecalis, S. Typhimurium and Listeria monocytogenes GH family 18 chitinases were inactive in this regard (Leisner et al, 2009;Larsen et al, 2011). It is of interest that the bacterial GH family 19 chitinases include a group annotated as having similarities with the lysozymes belonging to the lysozyme superfamily (Fig.…”

Section: Substrate Specificities Of Catalytic Domains Relevant To Virmentioning

confidence: 99%

Bacterial chitinases and chitin-binding proteins as virulence factors

et al. 2013

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“…These chitinases included 3 proteins from bacterial species, ChiS from Bacillus pumilus SG2 16 and FI and FII from Pseudomonas aeruginosa K-187, 17 2 proteins from fungi species, Aspergillus terreus 18 and Monascus purpureus CCRC31499, 19 and one protein (CpCHI) from papaya (Carica papaya). 20 In most of these papers (4 out of 5), the antibacterial activity of the protein was determined using the agar disk-diffusion method, whereas in one of them, 20 the authors used a dilution method.…”

Section: Resultsmentioning

confidence: 99%

“…31 This may explain previous results in which ChiS chitinase showed lysozyme activity towards 6 bacterial species, but only 2 of these species were killed by the same enzyme. 16 Concerning the potential exploitation of antibacterial chitinases as antimicrobial agents, the GH18 enzymes are particularly interesting, because they are likely to degrade bacterial cell walls using a mechanism that is distinct from that used by lysozymes. This possibility seems very attractive when we consider that some human pathogenic bacteria, such S. aureus and other species, are resistant to lysozyme.…”

Section: P Aeruginosa S Aureus and Salmonella Typhimentioning

confidence: 99%