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Purification and some properties of chitinase fromAspergillus carneus

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Abstract

An extracellular chitinase fromAspergillus cerneus was purified by ammonium sulphate precipitation, gel filtration through Sephadex G-100, preparative HPLC chromatography and large slabs of polyacry-lamide gel electrophoresis.The mol wt of the enzyme was estimated to be 25000 by SDS gel electrophoresis, and it contained 9.37% (w/w) carbohydrate residue, as glucose. The pattern of its amino acid composition showed high contents of asparagine, serine, and threonine. The enzyme was active at pH 5.2 and 50°C. The Km value of the enzyme was 4.37 mM (expressed asN-acetylglucosamine). The enzyme was stable at pH 3–9, whereas it was unstable at 70°C or more. Calcium and Mg ions slightly activated the enzyme, whereas Hg2+, I2, andp-chloromercuribenzoate inhibited the enzyme activity. The enzyme hydrolyzed chitin, colloidal chitin, glycol chitin, and chitooligsac-charides, but did not hydrolyze chitosan, starch, xylan, inulin, and cellulose. The lysis ofA. niger and Micorcoccus lysodeikticus cell walls by the action of the enzyme was also investigated.

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Abdel-Naby, M.A., El-Shayeb, N.M.A. & Sherief, A.A. Purification and some properties of chitinase fromAspergillus carneus . Appl Biochem Biotechnol 37, 141–154 (1992). https://doi.org/10.1007/BF02921666

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  • DOI: https://doi.org/10.1007/BF02921666

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