Bioconversion of Colloidal Chitin Using Novel Chitinase from Glutamicibacter uratoxydans Exhibiting Anti-fungal Potential by Hydrolyzing Chitin Within Fungal Cell Wall
- 48 Downloads
Chitin is a unique structural exopolysaccharide abundantly found in nature. This exopolysaccharide has a unique chemical structure that acts as a protective outermost covering for most of the crustaceans in aquatic ecosystem. This fortification is because of the insoluble nature of this exopolysaccharide which consist of a linear chain of β-(1→4)-linked-N-acetylglucosamine units. Chitin is hydrolyzed with the help of a hydrolase known as chitinase. Variety of microbial species have been explored for chitinase production. Chitinolytic microbial species can be alternatively used for degradation of chitin instead of chemical treatment in agricultural sector. This biological approach has lesser environmental impact because of its apparently safe nature.
In the current study, bioprospecting of chitinase producing species was conducted and different chitinolytic bacterial strains were screened for chitinase production which could have anti-fungal potential. Bacterial isolates were identified based on polyphasic approach and the enzyme production was optimized using one-variable-at-a-time technique. Hyphal extension method was used for determination of anti-fungal potential of chitinase.Glutamicibacter uratoxydans was indigenously isolated and identified for chitinase production. G. uratoxydans is a novel bacterial species which has not been previously explored to produce chitinase or other hydrolases. G. uratoxydans biosynthesized chitinase utilizing colloidal chitin as a sole source of carbon. The chitinase biosynthesized by G. uratoxydans is effectively potent against Aspergillus fumigatus thus, suggesting that this extracellular enzyme could be used for the treatment of fungal infection caused by filamentous fungi.
KeywordsColloidal chitin N-Acetyl-β-d-glucosamine Chitinase Glutamicibacter uratoxydans
Current research work was funded by Higher Education Commission (HEC), Islamabad, Pakistan through HEC-NRPU-Research Project No. 6549/Sindh/NRPU/R&D/2015.
Compliance with Ethical Standards
Conflict of interest
The authors declare that they have no conflict of interest.
This article doesn’t contain any studies with human participants or animals.
Informed consent was obtained from all the individual participants included in the current study.
- 1.Elieh-Ali-Komi, D., Hamblin, R.H.: Chitin and chitosan: production and application of versatile biomedical nanomaterials. Int. J. Adv. Res. 4, 411–427 (2016)Google Scholar
- 2.Chernin, L., Chet, I.: Enzymes in the Environment: Activity, Ecology and Applications. Taylor & Francis, CRC Press, New York (2002)Google Scholar
- 9.Husson, E., Hadad, C., Huet, G., Laclef, S., Lesur, D., Lambertyn, V., Jamali, A., Gottis, S., Sarazin, C., Nhien, A.N.V.: The effect of room temperature ionic liquids on the selective biocatalytic hydrolysis of chitin via sequential or simultaneous strategies. Green Chem. 19, 4122–4131 (2017)CrossRefGoogle Scholar
- 17.Whitman, W., Goodfellow, M., Kampfer, P., Busse, J.H., Trujillo, M., Ludwig, W., Suzuki, K.: Bergey’s Manual of Systematic Bacteriology. Springer, New York (2012)Google Scholar
- 18.Murthy, N., Bleakley, B.: Simplified method of preparing colloidal chitin used for screening of chitinase-producing microorganisms. Int. J. Microbiol. (2012) http://ispub.com/IJMB/10/2/14186
- 20.Lowry, O.H., Rosembrough, N.J., Fari, A.L., Randall, R.J.: Protein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265–275 (1951)Google Scholar
- 28.Busse, H.J.: Review of the taxonomy of the genus Arthrobacter, emendation of the genus Arthrobacter sensu lato, proposal to reclassify selected species of the genus Arthrobacter in the novel genera Glutamicibacter gen. nov., Paeniglutamicibacter gen. nov., Pseudoglutamicibacter gen. nov., Paenarthrobacter gen. nov., and Pseudoarthrobacter gen. nov., and emended descripition of Arthrobacter reseus. Int. J. Syst. Evol. Microbiol. 66, 09–37 (2016)CrossRefGoogle Scholar
- 32.Mejia-Saules, J.M., Waliszewski, K.N., Garcia, M.A., Cruz-Camarillo, R.: The use of crude shrimp shell powder for chitinase production by Serratia marcescens WF. Food Technol. Biotechnol. 44, 95–100 (2006)Google Scholar
- 33.Brzezinska, M.S., Walczak, M., Lalke-Porczyk, E., Donderski, W.: Utilization of shrimp shell waste as a substrate for the activity of chitinases produced by microorganisms. Pol. J. Environ. Stud. 19, 177–182 (2010)Google Scholar
- 45.Cano-Salazar, L., Gregorio-Jáuregui, K.M., Juárez-Ordaz, A.J., Leon-Joublanc, E., Perez-Molina, A., Martínez-Hernández, J.L., Rodríguez-Martínez, J., Ilyina, A.: Thermodynamics of partitioning of chitinase and laminarinase in a soya lecithin liposome system and their antifungal effect against Fusarium oxysporum. Biocatal. Biotransfor. 29, 60–70 (2011)CrossRefGoogle Scholar
- 55.Hollensteiner, J., Wemheuer, F., Harting, R., Kolarzyk, A.M., Diaz-Valerio, S.M., Poehlein, A., Brzuszkiewicz, E.B., Nesemann, K., Braus-Stromeyer, S.A., Braus, G.H., Daniel, R., Liesegang, H.: Bacillus thuringiensis and Bacillus weihenstephanensis inhibit the growth of phytopathogenic Verticillium species. Front. Microbiol. 7, 2171 (2017)CrossRefGoogle Scholar
- 59.Someya, N., Nakajima, M., Hirayae, K., Hibi, T., Akutsu, K.: Synergistic antifungal activity of chitinolytic enzymes and prodigiosin produced by biocontrol bacterium, Serratia marcescens Strain B2 against gray mold pathogen, Botrytis cinereal. J. Gen. Plant Pathol. 67, 312–317 (2001)CrossRefGoogle Scholar