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Puriflcation and properties of chitin deacetylase from Absidiaorchidis
Subtitle:Puriflcation and properties of chitin deacetylase from Absidiaorchidis
Creator:Szewczyk, Krzysztof W. ; Orzeszak, Małgorzata
Publisher:Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS
Date issued/created: Subject and Keywords: Abstract:Methods of purification of chitin deacetylase are discussed. A two stepmethod of purification of chitin deacetylase from mycelial extracts ofthe fungusAbsidia orchidis by chromatography is presented. The crude enzyme extract waspurified by a gel chromatography and then by ion exchange chromatography.Specific activity of purified enzyme was 12.3 U/mg and final purification degreewas 147. The apparent molecular mass of the enzyme was 75 kDa. When 0 -hydroxyethylated chitin (glycol chitin) was used as a substrate, the optimum pHfor enzyme activity was 5,5 and the optimum temperature was 50°C
Relation:Biotechnologia, vol.57, 2 (2002)-.
Volume: Issue: Start page: End page: Resource type: Detailed Resource Type: Format: Resource Identifier: Source:Library of Institute of Bioorganic Chemistry PAS
Language: Language of abstract: Temporal coverage: Rights:Creative Commons Attribution BY-SA 4.0 license
Terms of use: Digitizing institution:Institute of Bioorganic Chemistry of the Polish Academy of Science
Original in:Institute of Bioorganic Chemistry of the Polish Academy of Science
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