Novel lipase purification methods - a review of the latest developments

Biotechnol J. 2015 Jan;10(1):31-44. doi: 10.1002/biot.201400301. Epub 2014 Oct 2.

Abstract

Microbial lipases are popular biocatalysts due to their ability to catalyse diverse reactions such as hydrolysis, esterification, and acidolysis. Lipases function efficiently on various substrates in aqueous and non-aqueous media. Lipases are chemo-, regio-, and enantio-specific, and are useful in various industries, including those manufacturing food, detergents, and pharmaceuticals. A large number of lipases from fungal and bacterial sources have been isolated and purified to homogeneity. This success is attributed to the development of both conventional and novel purification techniques. This review highlights the use of these techniques in lipase purification, including conventional techniques such as: (i) ammonium sulphate fractionation; (ii) ion-exchange; (iii) gel filtration and affinity chromatography; as well as novel techniques such as (iv) reverse micellar system; (v) membrane processes; (vi) immunopurification; (vi) aqueous two-phase system; and (vii) aqueous two-phase floatation. A summary of the purification schemes for various bacterial and fungal lipases are also provided.

Keywords: Aqueous two-phase system; Lipase purification; Microbial lipases; Reverse micellar system.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism
  • Chemical Precipitation*
  • Chromatography / methods*
  • Fungal Proteins / chemistry
  • Fungal Proteins / isolation & purification
  • Fungal Proteins / metabolism
  • Lipase / chemistry
  • Lipase / isolation & purification*
  • Lipase / metabolism
  • Membranes, Artificial
  • Micelles

Substances

  • Bacterial Proteins
  • Fungal Proteins
  • Membranes, Artificial
  • Micelles
  • Lipase