Partial purification and properties of extracellular chitinase produced by Acremonium obclavatum, an antagonist to the groundnut rust, Puccinia arachidis

Gunaratna, K.R.; Balasubramanian, R.

doi:10.1007/bf00414876

Cited by 19 publications

(5 citation statements)

References 16 publications

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“…Seafood waste is today assuming major proportions and needs methods to be treated, for which chitinases hold great potential. Breakdown products such as chitosan are also increasingly finding application in several industries and methods to obtain them by enzymatic action are finding greater significance . Today there is a great focus on organisms and enzymes that can tolerate and function in extreme environments of temperature and pH and there are very scant reports on chitinases of such kind .…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of alkaline chitinase from Paenibacillus pasadenensis NCIM 5434

Loni

Patil

Phugare³

et al. 2014

J. Basic Microbiol.

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An alkaline chitinase was purified from the bacterium Paenibacillus pasadenensis NCIM 5434 isolated from alkaline littoral soil of Lonar Lake. The chitinase was purified by ammonium sulfate precipitation followed by DEAE cellulose column chromatography. Enzyme was purified by 8.87 folds with 24.96% yield. Molecular characterization through SDS-PAGE analysis showed that it has molecular weight of about ∼35 kDa. The enzyme kinetics studies of purified chitinase revealed the following characteristics, Km 6.25 mg ml(-1) and Vmax 434.78 µM for colloidal chitin as a substrate. The chitinase showed optimum pH 10 and temperature 37 °C. The enzyme exhibited significant activity up to 3% salt concentration, indicating saline nature. Its activity was enhanced with calcium, potassium and magnesium; whereas copper and mercury were found to be inhibitory. Since, it showed antifungal activity against Penicillium and Aspergillus, it could be used as powerful biocontrol agent.

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Section: Introductionmentioning

confidence: 99%

Purification and characterization of alkaline chitinase from Paenibacillus pasadenensis NCIM 5434

Loni

Patil

Phugare³

et al. 2014

J. Basic Microbiol.

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“…Through the degradation of the chitin polymer in the cell walls of fungal pathogens, chitinase (EC 3.2.1.14) plays a vital role in the biological control of many plant diseases (Haran et al 1993). It affects fungal growth through lysis of the cell walls (Kunz et al 1992), hyphal tips, and germ tubes (Gunarantna and Balasubramanian 1994). Many chitinases have been isolated (Han et al 2000;Baek et al 2001), and several genes from a variety of bacteria that encode these enzymes have also been cloned (Robbins et al 1992;Tsujibo et al 1993).…”

Section: Introductionmentioning

confidence: 99%

Antifungal chitinases from Bacillus pumilus SG2: preliminary report

Ghasemi

Ahmadian

Jelodar

et al. 2010

World J Microbiol Biotechnol

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A halotolerant bacterium capable of chitinase production was previously isolated from saline soils of Gavkhooni marsh, Iran. The strain was identified as Bacillus pumilus strain SG2. This strain secretes two chitinases into the medium in response to the presence of chitin in the medium. The two chitinases, ChiS and ChiL, were active on both polymeric as well as oligosaccharide substrates. In this study, these two extracellular chitinases were purified from the supernatant of the Bacillus culture by ammonium sulfate precipitation. The optimum pH and temperature for both of these chitinases were pH 6 and 37°C, respectively. According to the conserved domain analysis, ChiS and ChiL were categorized in family 18 of the glycosylhydrolases. Three essential conserved amino acid residues in in ChiL were found within the active site. Antifungal activities of the two purified chitinases were assessed on Rhizoctonia solani, Verticillium sp., Nigrospora sp., Stemphyllium botryosum and Bipolaris sp. demonstrating inhibition of all the tested strains. However, these chitinases did not inhibit cell wall formation of the non-chitin-containing fungi (oomycetes) Phytophthora citricola and Phytophthora capsici. This is the first investigation demonstrating antifungal activity of chitinases purified from B. pumilus SG2.

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“…Among these, chitinase (EC 3.2.1.14) plays a vital role in the biological control of many plant diseases by degrading the chitin polymer in the cell walls of fungal pathogens (Haran et al, 1993). It affects fungal growth through the lysis of cell walls (Kunz et al, 1992), hypal tips, and germ tubes (Gunarantna and Balasubramanian 1994). Many chitinases have been isolated (Han et al, 2000;Baek et al, 2001), and several genes that encode these enzymes have also been cloned from a variety of bacteria (Robbins et al, 1992;Tsujibo et al, 1993).…”

Section: Introductionmentioning

confidence: 99%