Bacterial Chitinases: Properties and Potential

Bhattacharya, Debaditya; Nagpure, Anand; Gupta, Rajinder K.

doi:10.1080/07388550601168223

Cited by 367 publications

(207 citation statements)

References 78 publications

Supporting

Mentioning

196

Contrasting

Unclassified

Order By: Relevance

“…This result was in agreement with other reports that chitin-binding proteins play an important role in the protection of plants against pathogen infection 27,28 . The mechanisms against fungal attack of chitin-binding proteins was supposed to take part in degrading chitin and/or adhering to the chitinous surfaces of the host cells 29,30 . Because Bacillus-derived compounds are the predominant class of antibiotics 31 , several studies examined the effects of heat, pH, and proteolytic enzymes (proteinase K and trypsin) on the activity of antifungal compounds produced by Bacillus sp.…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of an antifungal protein from Bacillus subtilis XL62 isolated in Vietnam

Tuyen¹,

Le²,

Nguyen³

et al. 2017

ScienceAsia

View full text Add to dashboard Cite

ABSTRACT:Bacillus subtilis is considered as a potential antagonist for fungal control due to its ability to produce a wide range of antibiotics. This study determines the antifungal activity of the native B. subtilis XL62 and we purify, identify, and characterize the antifungal protein. The results show that the growth inhibitory activity to Fusarium oxysporum and Rhizoctonia solani of the crude supernatant of B. subtilis XL62 was proportional to the concentration. At the highest concentration (50%), the growth inhibition reached 90% and 100% for F. oxysporum, and R. solani, respectively. Furthermore, the crude supernatant of B. subtilis XL62 also inhibited the germination and growth of R. solani. The growth of sclerotia was almost completely inhibited at the concentration of 20% and the ability to germinate was lost at the concentration of 50%. Antifungal proteins were isolated from the crude bacterial supernatant using ammonium sulphate precipitation followed by passage over DEAE-cellulose and Biogel P100 columns. The purified protein had an apparent molecular mass of 22 kDa. Its antifungal activity was retained even at 100°C, for 60 min and after treatment with proteinase K (0.5-2.5 µg/ml). The results of protein identification using a MALDI-TOF/TOF mass spectrometer suggest that the purified protein is indeed a chitin-binding protein.

show abstract

Section: Discussionmentioning

confidence: 99%

Purification and characterization of an antifungal protein from Bacillus subtilis XL62 isolated in Vietnam

Tuyen¹,

Le²,

Nguyen³

et al. 2017

ScienceAsia

View full text Add to dashboard Cite

show abstract

“…Bacterial chitinases serve to degrade chitin for carbon and nitrogen sources to support growth [52]. It has recently become clear that representatives of both Gram-positive and Gram-negative bacterial pathogens encode chitinases and CBPs that support infection of non-chitinous mammalian hosts [53].…”

Section: Chitin-engasesmentioning

confidence: 99%

Endo-N-Acetyl-β-D-Glucosaminidases and Peptide-N4-(N-acetyl-β-D-Glucosaminyl) Asparagine Amidases: More Than Just Tools

Karamanos¹

2013

View full text Add to dashboard Cite

Abstract:Since the discovery of endo-N-acetyl-β-D-glucosaminidases (ENGase) and peptide-N4-(N-acetyl-β-D-glucosaminyl) asparagine amidases (PNGase) most of the published work described their use for structural studies. Less attention was given to the potential roles of those enzymes in the physiology of the cells/organisms they produced them. The scope of this review is firstly to analyse the data on the occurrence and characteristics of murein-, chitin-, and N-glycan-ENGases acting on GlcNAc-containing polymers in three structural families, namely murein, chitin, and N-glycosylproteins, and of PNGases, only acting on N-glycosylproteins, and secondly to discuss the biological roles of the enzymes in the producing cells. The analysis demonstrates the remarkable diversity of the enzymes, and simultaneously the interest of studying their substrate specificity and their structural features. Many examples illustrate the importance of the structure/function relationships studies. Diverse biological roles were anticipated, e.g. they are useful for feeding purposes, are implicated in pathogenesis processes, modulate the activity of macromolecules, and help in the destruction of misfolded proteins. Their effect can be direct or indirect, through the reaction products. Current knowledge only partially explains the biological roles of ENGases and PNGases, thus further studies are expected for determining novel possibilities and elucidating other cell pathways.

show abstract

“…Chitinases (E.C. 3.2.1.14) are a group of enzymes capable of hydrolysing insoluble chitin to its oligo (chitosan and chitobiose) and monomeric (N-acetylglucosamine) components (Bhattacharya et al 2007). Chitinases occur in a wide range of organisms including viruses, bacteria, fungi, insects, higher plants and animals for offensive, defensive, morphogenetic or nutritional purposes (Park et al 1997;Dahiya et al 2006).…”

Section: Introductionmentioning

confidence: 99%

A novel halo-alkali-tolerant and thermo-tolerant chitinase from Pseudoalteromonas sp. DC14 isolated from the Caspian Sea

Makhdoumi

Dehghani-Joybari

Mashreghi

et al. 2015

Int. J. Environ. Sci. Technol.

View full text Add to dashboard Cite

A novel halo-alkali and thermo-tolerant chitinase was obtained from an isolated strain found in the Caspian Sea. The effects of media composition and various fermentation conditions for the optimization of chitinase production were studied one factor at a time and by response surface methodology. The novel strain, which is designated as strain DC14 and phylogenetically related to the genus Pseudoalteromonas, produced chitinase after 72 h under the following optimal conditions: glucose 1 % (w/v), ammonium sulphate 0.2 % (w/v), chitin 1.07 % (w/ v), pH 8, NaCl 10 % (w/v), inoculums size 2.5 % (v/v), temperature 30°C, CaCl 2 3 mM and MgCl 2 4 mM. Using the statistical optimization method, chitinase production was found to increase from 2.30 to 21.90 U/dl. The enzyme showed maximum activity at 40°C, pH 9 and 10 % NaCl. It was stable in a wide range of temperature from 15 to 65°C, pH from pH 7 to 11 and NaCl concentration from 0 to 15 % (w/v). The molecular weight of the enzyme was estimated by SDS-PAGE to be about 65 kDa. With regard to the halo-alkali and thermo-stable properties of this enzyme, it has potential industrial activity.

show abstract

Bacterial Chitinases: Properties and Potential

Cited by 367 publications

References 78 publications

Purification and characterization of an antifungal protein from Bacillus subtilis XL62 isolated in Vietnam

Purification and characterization of an antifungal protein from Bacillus subtilis XL62 isolated in Vietnam

Endo-N-Acetyl-β-D-Glucosaminidases and Peptide-N4-(N-acetyl-β-D-Glucosaminyl) Asparagine Amidases: More Than Just Tools

A novel halo-alkali-tolerant and thermo-tolerant chitinase from Pseudoalteromonas sp. DC14 isolated from the Caspian Sea

Contact Info

Product

Resources

About