Purification and properties of Amycolatopsis mediterranei DSM 43304 lipase and its potential in flavour ester synthesis

Dheeman, D. S., Henehan, G. T.M. and Frías, J. M. (2011) Purification and properties of Amycolatopsis mediterranei DSM 43304 lipase and its potential in flavour ester synthesis. Bioresource Technology, 102(3), pp. 3373-3379. (doi: 10.1016/j.biortech.2010.11.074) (PMID:21145735)

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Abstract

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 K(m)(app) and V(max)(app) for p-nitrophenyl palmitate (p-NPP) at the optimal temperature (60°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.

Item Type:Articles (Other)
Additional Information:This work was financially supported by DIT ABBEST Research Scholarship (PB 03557/2007) to DSD.
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Dheeman, Dr Dharmendra
Authors: Dheeman, D. S., Henehan, G. T.M., and Frías, J. M.
College/School:College of Medical Veterinary and Life Sciences > School of Infection & Immunity
Journal Name:Bioresource Technology
Publisher:Elsevier
ISSN:0960-8524
Published Online:21 November 2010

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