Isolation and identification of two novel SDS‐resistant secreted chitinases from <i>Aeromonas schubertii</i>

Liu, Chao Lin; Shen, Chia-Rui; Hsu, Fong‐Fu; Chen, Jeen Kuan; Wu, Pei Tzu; Guo, Shang Hsin; Lee, Wen Chien; Yu, Feng; Mackey, Zachary B.; Turk, John; Gross, Michael L.

doi:10.1002/btpr.100

Cited by 29 publications

(21 citation statements)

References 59 publications

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“…), 53 KDa for ASCHI53 and 61 KDa for ASCHI61 form Aeromonas schubertii (Liu et al . ). Generally, the molecular weight of chitinase was ranged from 20 to 80 kDa.…”

Section: Discussionmentioning

confidence: 97%

Partial purification and characterization of chiIO8, a novel antifungal chitinase produced by Bacillus cereus IO8

Hammami¹,

Siala

Jridi

et al. 2013

J Appl Microbiol

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Aims: To investigate the distribution of chitinase IO8 in Bacillus cereus strains, the enhancing effects of the chitinase-producing B. cereus strains on biocontrol potential by dual culture assay and in vivo assay against Botrytis cinerea and also the enhancing effects of the chiIO8 on disinfectant properties against seedborne diseases. Moreover, the application of chiIO8 treatment was also observed to improve the germinative energy. Methods and Results: The purification steps included ammonium sulfate precipitation, with columns of DEAE-Sepharose anion-exchange chromatography and Sephacryl S-400 high-resolution gel chromatography. The method gave a 5Á8-fold increase in the specific activity and had a yield of 17%. The molecular weight of the partially purified chitinase chiIO8 was found to be around 30 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimal pH and optimal temperature of the partially purified chitinase were pH 6Á5 and 65°C, respectively. The thermostable chitinase still retained the activity after incubation for 100 min at 65°C, and it was increased about 1Á25 times than that of the control (before heating) when the enzyme solution heated at 65°C for 60 min. The partially purified chitinase chiIO8 displays a wide inhibitory spectrum towards all phytopathogenic fungi tested. chiIO8 also exhibited effective disinfectant properties against seed-borne diseases. Conclusion: The present investigation emphasizes the potential of chitinaseproducing micro-organism as promising biocontrol agents of fungal plant pathogens with chitinous cell wall. The novel chitinase chiIO8 proved an efficient, environmentally safe and user-friendly solution. Significance and Impact of the Study: This is the first investigation devoted exclusively to analyse the distribution of chitinase in B. cereus. It infers that the chitinase produced by B. cereus might play a role in the activity of the biopesticide.

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“…), 53 KDa for ASCHI53 and 61 KDa for ASCHI61 form Aeromonas schubertii (Liu et al . ). Generally, the molecular weight of chitinase was ranged from 20 to 80 kDa.…”

Section: Discussionmentioning

confidence: 97%

Partial purification and characterization of chiIO8, a novel antifungal chitinase produced by Bacillus cereus IO8

Hammami¹,

Siala

Jridi

et al. 2013

J Appl Microbiol

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“…The molecular mass of the chitinase produced by L. capsici YS 1215 was estimated to be 43.6 kDa, similar to previous reports in which the molecular masses of chitinases secreted by Sanguibacter antarcticus KOPRI 21702, Pénicillium sp. LYG0704, Aeromonas schubertii ASCHI53 and A. schubertii ASCHI61 were estimated to be 55, 47, 53 and 61 kDa, respectively (Liu et al, 2009;Park et al, 2009).…”

Section: Discussionmentioning

confidence: 97%

Purification and properties of a Meloidogyne-antagonistic chitinase from Lysobacter capsici YS1215

Lee

Anees

Park

et al. 2014

Nematol

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The root-knot nematodes, Meloidogyne spp., cause serious diseases in various plants and their chemical control may lead to environmental problems. Therefore, alternative control measures against the phytopathogenic nematodes are being sought. One of the potential targets against Meloidogyne spp. may be the chitinolysis and degradation of nematode eggs. Therefore, in the present study, a chitinolytic and nematicidal strain of Lysobacter capsici YS1215 was isolated from an agricultural field in Korea. The aim of this study was to purify chitinase secreted by L. capsici YS1215 and investigate its nematicidal role against Meloidogyne incognita. The chitinase secreted by L. capsici YS1215 was purified by protein precipitation with 80% ammonium sulphate, anion-exchange chromatography with DEAE-cellulose and gel-filtration chromatography with Sephadex G-100. By chitinase-active staining of the purified enzyme, a single band was obtained with an estimated molecular mass of 43.6 kDa. The optimal pH and optimal temperature for the highest chitinase activity were 6.0 and 40°C, respectively. The purified chitinase degraded the chitin layer of the eggshells and significantly reduced hatch of second-stage juveniles. The activity of chitinase secreted by L. cap.úci YS1215 was not affected by CoCh, MnCl2, MgCl2, CUSO4, CaCl2 or EDTA. The purified enzyme could also hydrolyse swollen chitin, glycol chitin, glycol chitosan and chitin powder Thus, the role of chitinase secreted by L. capsici YS1215 against Meloidogyne spp. may be useful for further development of a biocontrol agent.

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“…The mutant enzyme showed higher activity, as also thermal and pH stabilities. Liu et al isolated two SDS‐resistant endochitinases, from Aeromonas schubertii . The denaturation‐resistant enzymes can have rigid structures that can overcome the complexity of the substrate for a variety of applications.…”

Section: Introductionmentioning

confidence: 99%

Chitinolytic enzymes: An appraisal as a product of commercial potential

Chavan

Deshpande

2013

Biotechnology Progress

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Chitin, its deacetylated form, chitosan and chitinolytic enzymes viz. endo-chitinase, N-acetylglucosaminidase, chitosanase, chitin deacetylase (CDA) are gaining importance for their biotechnological applications. Presently, chitin degrading enzymes constitute high-cost low-volume products in human health care and associated research. Indeed chitinases and CDA-chitosanase complex possesss tremendous potential in agriculture to control plant pathogenic fungi and insects. The success in exploring chitinases especially for agriculture, i.e. as a high-volume low-cost product, depends on the availability of highly active preparations with a reasonable cost. Therefore, a reconsideration in terms of understanding the roles of chitinolytic enzymes in applications, e.g. host-pathogen interaction for biocontrol, different mechanisms of chitin degradation, and identification of new enzymes with varying specificities, may make them more useful in a variety of commercial processes in the near future. The possible issues and challenges encountered in the translation of proof of concept into a commercial product will be appraised in this review.

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Isolation and identification of two novel SDS‐resistant secreted chitinases from Aeromonas schubertii

Cited by 29 publications

References 59 publications

Partial purification and characterization of chiIO8, a novel antifungal chitinase produced by Bacillus cereus IO8

Partial purification and characterization of chiIO8, a novel antifungal chitinase produced by Bacillus cereus IO8

Purification and properties of a Meloidogyne-antagonistic chitinase from Lysobacter capsici YS1215

Chitinolytic enzymes: An appraisal as a product of commercial potential

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