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Purification and some properties of ɛ-poly-l-lysine-degrading enzyme from Kitasatospora sp. CCTCC M205012

Paper ID Volume ID Publish Year Pages File Format Full-Text
35851 45110 2008 6 PDF Available
Title
Purification and some properties of ɛ-poly-l-lysine-degrading enzyme from Kitasatospora sp. CCTCC M205012
Abstract

An ɛ-poly-l-lysine-degrading enzyme (PLD) from Kitasatospora sp. CCTCC M205012 has been purified to homogeneity by three steps of anion-exchange chromatography including DEAE-Sepharose, Source 15Q and Mono Q, with a 500-fold increase in specific activity and 40.9% yield. The PLD has a molecular mass of approximately 87.0 kDa and consists of two identical subunits with a molecular mass of 43.6 kDa. Electrophoretic shows that the PLD isoelectric point was about 7.2. The optimum temperature and pH for the PLD was 30 °C and 7.0, respectively. The PLD was deactivated by EDTA, which was indicated that the enzyme was a metallo enzyme. The activity of PLD was stimulated by Co2+ and inhibited by Ca2+ remarkably. The apparent Km with l-lysyl-p-nitroanilide as substrate was 0.216 mM and the Vmax was 0.112 mmol/min mg. The PLD was an exo-type enzyme and monomers of l-lysine were detected during the enzymatic degradation of ɛ-PL.

Keywords
ɛ-Poly-l-lysine-degrading enzyme; Kitasatospora sp. CCTCC M205012; Purification; Anion-exchange chromatography; Properties; Degradation
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Purification and some properties of ɛ-poly-l-lysine-degrading enzyme from Kitasatospora sp. CCTCC M205012
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 6, June 2008, Pages 667–672
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
You save - $31
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