Journal
BIORESOURCE TECHNOLOGY
Volume 102, Issue 3, Pages 3373-3379Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.biortech.2010.11.074
Keywords
Actinomycete lipase; Amycolatopsis mediterranei; Purification; Characterization; Ester synthesis
Funding
- DIT ABBEST Research Scholarship [PB 03557/2007]
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An extracellular thermostable lipase from Amycolatopsis mediterranei DSM 43304 has been purified to homogeneity using ammonium sulphate precipitation followed by anion exchange chromatography and hydrophobic interaction chromatography. This protocol resulted in a 398-fold purification with 36% final recovery. The purified A. mediterranei DSM 43304 lipase (AML) has an apparent molecular mass of 33 kDa. The N-terminal sequence, AANPYERGPDPTTASIEATR, showed highest similarity to a lipase from Streptomyces exfoliatus. The values of f(m)(app) and V-max(app) for p-nitrophenyl palmitate (p-NPP) at the optimal temperature (60 degrees C) and pH (8.0) were 0.099 +/- 0.010 mM and 2.53 +/- 0.06 mmol/min mg, respectively. The purified AML displayed significant activity towards a range of short and long chain triglyceride substrates and p-nitrophenyl esters. Hydrolysis of glycerol ester bonds occurred non-specifically. The purified AML displayed significant stability in the presence of organic solvents (40%, v/v) and catalyzed the synthesis of the flavour ester isoamyl acetate in free and immobilized states. (C) 2010 Elsevier Ltd. All rights reserved.
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