Functional expression of Rhizopus oryzae lipase in Pichia pastoris: High-level production and some properties

Stefan Minning, Claudia Schmidt-Dannert, Rolf D. Schmid

Research output: Contribution to journalArticlepeer-review

69 Scopus citations

Abstract

The mature lipase of the fungus Rhizopus oryzae (ROL) was functionally expressed and secreted in the methylotrophic yeast Pichia pastoris. In a batch cultivation, where methanol feeding was linked to the dissolved oxygen content in the cultivation solution, a lipase activity of 500 000 units per liter (60 mg active lipase per liter) of culture was achieved after initial glycerol feeding of the culture. Recombinant ROL lipase was purified to homogeneity by a simple two-step purification procedure and had a specific activity of 8571 U mg-1 (triolein, 30°C, pH 8.1) which is comparable with the purified native enzyme. The properties of the recombinant lipase were similar to those reported both for the native lipase and for the enzyme expressed in Escherichia coli and refolded from inactive inclusion bodies. Copyright (C) 1998 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)147-156
Number of pages10
JournalJournal of Biotechnology
Volume66
Issue number2-3
DOIs
StatePublished - Dec 11 1998

Bibliographical note

Funding Information:
We are grateful to Volker Noedinger for performing the protein sequencing, and we thank the European Community for financial support under contract Bio4-CT96-00005.

Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.

Keywords

  • Lipase
  • Pichia pastoris
  • Production
  • Properties
  • Purification
  • Rhizopus oryzae

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