Bacterial chitinase: nature and perspectives for sustainable bioproduction

Yan, Qiang; Fong, Stephen S.

doi:10.1186/s40643-015-0057-5

Cited by 59 publications

(40 citation statements)

References 61 publications

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“…Chitinases are produced by different microorganisms such as bacteria, fungi and algae and are involved in various biological processes as defense against pathogens, nutrition and morphogenesis (Yan & Fong, 2015). Commercially chitinolytic enzymes are used to produce NAG and chitooligosaccharides as part of pharmaceutical formulations.…”

Section: Introductionmentioning

confidence: 99%

Efficacy of Thermophilic Soil-Isolated Paenibacillus sp. NBR10 as a Chitinolytic and Biocontrol Bacterium-In vitro Study

et al. 2018

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A mONG microbial enzymes, chitinases received increased attentions due to their wide applications especially in agriculture sector for biocontrol of fungal phytopathogens. The growing interest in chitinases with thermostability nature, forced many researchers to isolate and characterize novel chitinase producing-bacteriafrom extreme environments. The present study describe characterization of thermostable chitinase produced by thermophilic soilisolated bacterial strain NBR10 from Rafha governorate, Saudi Arabia. Chitinase producing NBR10 strain was identified as Paenibacillus sp. according to the traditional methods of morphological, biochemical and physiological characteristics coupling with sequencing of 16S rRNA (GenBank accession number KT957624.1). The isolated strain was found to have a potent antifungal against three of the phytopathogenic fungi Fusarium oxysporum, Alternaria burnsii and Rhizoctonia solani with percent of growth inhibition 52.5 75.0 and 85.71%, respectively. Chitinase obtained from Paenibacillus sp. NBR10 showed activity at ranges of temperature (30-90°C) and pH (4-9), showing optimum activity at 55°C and pH 7.0, respectively. Also, it exhibited high thermostability at higher temperatures, where 90% of its activity is retained at 65°C for 36h. The promising chitinolytic and antifungal activity of locally isolated Paenibacillus sp. NBR10, candidate this strain to be used as a potential biological control agent.

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Section: Introductionmentioning

confidence: 99%

Efficacy of Thermophilic Soil-Isolated Paenibacillus sp. NBR10 as a Chitinolytic and Biocontrol Bacterium-In vitro Study

et al. 2018

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“…Moreover, chitin is increasingly being recognized as an important feedstock for the production of renewable chemicals, and chito-oligosaccharides are being investigated for several biomedical applications (3)(4)(5)(6). The strategies used by microbes for efficient chitin bioconversion are gaining interest, as current chemical methods used for the industrial processing of chitin are inefficient and wasteful (7,8). Therefore, the combination of environmental importance and industrial/medical relevance has renewed interest in the bioconversion of chitin (9,10).…”

mentioning

confidence: 99%

Systems analysis of the glycoside hydrolase family 18 enzymes from Cellvibrio japonicus characterizes essential chitin degradation functions

Monge

Tuveng

Vaaje‐Kolstad

et al. 2018

Journal of Biological Chemistry

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“…The best suited structure is chosen by the SWISS-MODEL and based on the sequence of that model a tentative three dimensional structure was made for the submitted sequence ( Figures 9 and 10). The 453 amino acid residues of isolate 130 were folded into a domain (β-jelly roll) structure comprising 3 antiparallel α-helices and five parallel β-sheets, like other enzymes belonging to the glycoside hydrolase family 18 (Watanabe et al, 1999, Hamid et al, 2013, Yan and Fong, 2015.…”

Section: Analysis Of Structure and Catalytic Sitesmentioning

confidence: 99%

Purification and molecular characterization of chitinases from soil actinomycetes

Das¹,

Kumar²,

Kumar³

et al. 2017

Afr. J. Microbiol. Res.

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Microbial extracellular chitinases are used in agriculture as effective biocontrol agents and in waste degradation, pharmaceutical and food industry. Actinomycetes are widely tapped group for production of extracellular chitinases. In the present study, approximately 260 actinomycetes were isolated from various ecological habitats was subjected to primary analyses and screened for production of chitinase by plate assay method. Diameter of zones of hydrolysis ranged from 8 to 16 mm. Based on the results, isolates 130, 194, 184, NRRLB 24916 (Streptomyces mexicanus) and NRRLB 16746 (Streptomyces albidoflavus, positive control) were selected for secondary screening and purification. Enzyme activity was estimated in crude cell free extract and partially purified samples. Activity ranged from 7.16 to 14.12 IU/ml (in crude extracts) and 12.1 to 23.10 IU/ml (in partially purified samples). In case of highest chitinase producing isolate 130, effect of various fermentation conditions (pH, temperature and substrate concentration) was studied in crude extract. Furthermore, complete purification of isolate 130 was done by column chromatography and the activity in purified fraction was found to be 32.12 IU/ml. The K m and V max values of the purified fractions for isolate 130 were 2.11 µg/ml/min and 53.11mg/ml respectively. This shows that the enzyme has high affinity for the substrate. SDS gel electrophoresis of the purified fraction showed presence of single band of approximately 65 to 70 kDa. Analyses of purified chitinase were done using MS/MS technique. N-terminal sequence corresponded to chitinase, the gene encodes a protein of 453 amino acid residues. Comparison of deduced amino acid sequence to other chitinases in the database indicated that enzyme showed 70% similarity with chitinase from Streptomyces plicatus and belongs to glycoside hydrolase family 18. Homology modeling showed that the enzyme was folded into a domain of (α/β) 8 barrel structure. Identification of secondary structure was done by CD spectroscopy. Isolate 130 was capable of degrading biodegradable wastes such as crustacean shells.

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Bacterial chitinase: nature and perspectives for sustainable bioproduction

Cited by 59 publications

References 61 publications

Efficacy of Thermophilic Soil-Isolated Paenibacillus sp. NBR10 as a Chitinolytic and Biocontrol Bacterium-In vitro Study

Efficacy of Thermophilic Soil-Isolated Paenibacillus sp. NBR10 as a Chitinolytic and Biocontrol Bacterium-In vitro Study

Systems analysis of the glycoside hydrolase family 18 enzymes from Cellvibrio japonicus characterizes essential chitin degradation functions

Purification and molecular characterization of chitinases from soil actinomycetes

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