publication . Article . 2012

Production of Antifungal Chitinase by Aspergillus niger LOCK 62 and Its Potential Role in the Biological Control

Maria Swiontek Brzezinska; Urszula Jankiewicz;
Open Access English
  • Published: 26 Aug 2012 Journal: Current Microbiology, volume 65, issue 6, pages 666-672 (issn: 0343-8651, Copyright policy)
  • Publisher: Springer Nature
Abstract
Aspergillus niger LOCK 62 produces an antifungal chitinase. Different sources of chitin in the medium were used to test the production of the chitinase. Chitinase production was most effective when colloidal chitin and shrimp shell were used as substrates. The optimum incubation period for chitinase production by Aspergillus niger LOCK 62 was 6 days. The chitinase was purified from the culture medium by fractionation with ammonium sulfate and affinity chromatography. The molecular mass of the purified enzyme was 43 kDa. The highest activity was obtained at 40 °C for both crude and purified enzymes. The crude chitinase activity was stable during 180 min incubatio...
Subjects
Medical Subject Headings: food and beveragesfungi
free text keywords: Applied Microbiology and Biotechnology, Microbiology, Article, General Medicine, Biology, Botrytis cinerea, biology.organism_classification, Aspergillus niger, Fusarium oxysporum, Rhizoctonia solani, Food science, Chitin, chemistry.chemical_compound, chemistry, Fusarium solani, Alternaria alternata, Chitinase, biology.protein
32 references, page 1 of 3

Adrangi, S, Faramarzi, MA, Shahverdi, AR, Sepehrizadeh, Z. Purification and characterization of two extracellular endochitinases from Massilia timonae. Carbohydr Res. 2010; 345: 402-407 [OpenAIRE] [PubMed] [DOI]

Ait-Lahsen, H, Soler, A, Rey, M, Cruz, J, Monte, E, Llobell, A. An antifungal exo-α-1,3-glucanase (AGN13.1) from the biocontrol fungus Trichoderma harzianum. Appl Environ Microbiol. 2001; 67: 5833-5839 [OpenAIRE] [PubMed] [DOI]

Binod, P, Pusztahely, T, Nagy, V, Sandhya, C, Szakàcs, G, Pócsi, I, Pandey, A. Production and purification of extracellular chitinases from Penicilliumaculeatum NRRL 2129 under solid-state fermentation. Enzym Microbiol Technol. 2005; 36: 880-887 [OpenAIRE] [DOI]

Bradford, MM. Rapid and sensitive methods for the quantitation of microgram quantities of protein utilizing the principle of protein–dye binding. Anal Biochem. 1976; 72: 248-254 [OpenAIRE] [PubMed] [DOI]

Budi, SW, Tuinen, D, Arnould, C, Dumas-Gaudut, E, Gianinazzi-Pearson, V, Gianinazzi, S. Hydrolytic enzyme activity of Paenibacillus sp. strain B2 and effect of antagonistic bacterium on cell wall integrity of two soil-borne pathogenic fungi. Appl Soil Ecol. 2000; 15: 191-199 [DOI]

Deshpande, MV. Mycopesticide production by fermentation: potential and challenges. Crit Rev Microbiol. 1999; 25: 229-243 [OpenAIRE] [PubMed] [DOI]

Escott, GM, Hearn, VM, Adams, DJ. Inducible chitinolytic system of Aspergillus fumigatus. Microbiology. 1998; 144: 1575-1581 [OpenAIRE] [PubMed] [DOI]

Gohel, V, Singh, A, Vimal, M, Ashwini, P, Chatpar, HS. Bioprospecting and antifungal potential of chitynolitic microorganisms. Afr J Biotechnol. 2006; 5: 54-72 [OpenAIRE]

Gooday, GW. The many uses of chitinases in nature. Chitin Chitosan Res. 1997; 3: 233-243

Hoppe, HG, Sherr, BF, Cole, JJ, Kemp, PF. Use of fluorogenic model substrates for extracellular enzyme activity (EEA) measurements of bacteria. Handbook of methods in aquatic microbial ecology. 1993: 509-512

Howell, CR. Mechanisms employed by Trichoderma species in the biological control of plant diseases: the history and evolution of current concepts. Plant Dis. 2003; 87: 4-10 [DOI]

Joo, GJ. Purification and characterization of an extracellular chitinase from the antifungal biocontrol agent Streptomyces halstedii. Biotechnol Lett. 2005; 27: 1483-1486 [OpenAIRE] [PubMed] [DOI]

Kavitha, S, Senthilkumar, S, Gnanamanickam, S, Inayathullah, M, Jayakumar, R. Isolation and partial characterization of antifungal protein from Bacillus polymyxa strain VLB16. Process Biochem. 2005; 40: 3236-3243 [OpenAIRE] [DOI]

Kim, PI, Chung, KC. Production of an antifungal protein for control of Colletotrichum lagenarium by Bacillus amyloliquefaciens MET0908. FEMS Microbiol Lett. 2004; 234: 177-183 [OpenAIRE] [PubMed] [DOI]

Laemmli, UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227: 680-685 [OpenAIRE] [PubMed] [DOI]

32 references, page 1 of 3
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