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^: *https://onlinelibrary.wiley.com/loi/14390434 (https://onlinelibrary.wiley.com/loi/14390434)
^: Swiontek Brzezinska M.; Jankiewicz U.; Kalwasinska A. ; Swiatczak J.; Zero K.
^: Characterization of chitinase from Streptomyces luridiscabiei U05 and its antagonist potential against fungal plant pathogens [ , Streptomyces luridiscabiei U05, , Alternaria alternata, Fusarium oxysporum, F. solani, Botrytis cinerea, F. culmorum Penicillium verrucosum. ()]
^: Journal of Phytopathology, 2019; Vol.167,N 7-8. - P. 404-412
^: 2019
^: Bibliogr.:p.410-412
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^: Streptomyces luridiscabiei U05 was isolated from wheat rhizosphere. It produced chitinase, which showed in vitro antifungal properties. The crude enzyme inhibited the growth of Alternaria alternata, Fusarium oxysporum, F. solani, Botrytis cinerea, F. culmorum and Penicillium verrucosum. The chitinase enzyme of the molecular weight of 45 kDa was purified using affinity chromatography of chitin. Streptomyces luridiscabiei U05 produced different chitinolytic enzymes. The highest enzyme activity was observed with the use of 4-MU-(GlcNAc), which points to the presence of an β-N-acetylhexosaminidase. The optimum activity was obtained at 35-40C and pH 7-8. The enzyme showed thermostability at 35-40C during 240 min of preincubation and lost its activity at 50C and 60C in 60 min. The chitinase activity from S. luridiscabei U05 was strongly inhibited by Hg2+ and Pb2+ ions, and sodium dodecyl sulphate (SDS). The Ca2+, Cu2+ and Mg2+ ions stimulated the activity of the enzyme. aref1

^TRN: 1914111
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