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1

Purification and properties of chitin deacetylase from Absidia orchidis

100%
Szewczyk K. W., Orzeszak M.
Biotechnologia
|
2002
|
issue 2
48-59
EN
Methods of purification of chitin deacetylase are discussed. A two step method of purification of chitin deacetylase from mycelial extracts of the fungus Absidia orchidis by chromatography is presented. The crude enzyme extract was purified by a gel chromatography and then by ion exchange chromatography. Specific activity of purified enzyme was 12.3 U/mg and final purification degree was 147. The apparent molecular mass of the enzyme was 75 kDa. When O ? hydroxyethylated chitin (glycol chitin) was used as a substrate, the optimum pH for enzyme activity was 5,5 and the optimum temperature was 50?C.
2

Purification and some characteristics of Penicillium citrinum lipase

80%
Maliszewska I. H.
Biotechnologia
|
1997
|
issue 3
109-120
EN
An extracellular lipase (glycerol ester hydrolases E.C. 3.1.1.3.) was isolated from a culture filtrate of Penicillium citrinum. The purification procedure included ammonium sulfate precipitation, ultrafiltration and chromatography on Octyl-Sepharose CL-4B. The enzyme was 400-fold purified with 9.66% yield. The molecular weight has been estimated by polyacrylamide gel electrophoresis under denaturing conditions at 26000. On the other hand, lipase forms active dimers and tetramers aggregates as observed after native PAGE. Lipase from Penicillium citrinum showed a preference for triacylglycerols. It is non-specific and hydrolyzes each of the three ester bonds of triacylglycerols. The enzyme showed a maximum activity at pH 7.2 at 30 oC and was stable in the range of pH 6.0-7.5 and the temperature of 10oC - 40oC.
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