Subtitle:

Puriflcation and properties of chitin deacetylase from Absidiaorchidis

Publisher:

Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS

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:

57

Issue:

2

Start page:

48

End page:

59

Detailed Resource Type:

Article

Format:

application/pdf

Resource Identifier:

0860-7796 ; oai:rcin.org.pl:138077 ; IChB B-53

Source:

Library of Institute of Bioorganic Chemistry PAS

Language:

pol

Language of abstract:

eng

Temporal coverage:

1988-2010

Rights:

Creative Commons Attribution BY-SA 4.0 license

Terms of use:

Copyright-protected material. [CC BY-SA 4.0] May be used within the scope specified in Creative Commons Attribution BY-SA 4.0 license, full text available at:

Digitizing institution:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Original in:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Projects co-financed by:

Operational Program Digital Poland, 2014-2020, Measure 2.3: Digital accessibility and usefulness of public sector information; funds from the European Regional Development Fund and national co-financing from the state budget.

Access:

Open