Molecular cloning and characterization of a novel cold-active lipase from Pichia lynferdii NRRL Y-7723

Jae Han Bae, In Hwan Kim, Ki Teak Lee, Ching T. Hou, Hak Ryul Kim

Research output: Contribution to journalArticlepeer-review


Lipase is one of the widely used biocatalysts, which is well studied for its application in industrial production. Recently, lipases with special characteristics such as thermo-stability, alkaline-, acidic nature, and cold-activity, have gained attention for effective applications in specific purposes. Previously, Pichia lynferdii NRRL Y-7723 was reported to produce high amounts of extracellular cold-active lipase (Kim et al., 2010). In this study, we report the identification of lip1 gene that encodes an extracellular cold-active lipase from P. lynferdii NRRL Y-7723. The open reading frame of the gene consisted of 1122 bp of nucleotides that encoded a protein with 373 amino acids. The deduced molecular weight and isoelectric point were 41.8 kDa and pH 5.82, respectively. The lip1 gene was cloned into a bacterial expression vector, and the recombinant lipase was successfully expressed and purified. Several parameters of the recombinant lipase were analyzed, and Lip1 showed high activity at low temperature.

Original languageEnglish
Pages (from-to)19-25
Number of pages7
JournalBiocatalysis and Agricultural Biotechnology
Publication statusPublished - 2017 Jul

Bibliographical note

Funding Information:
This research was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (2010-0023701).

Publisher Copyright:
© 2017 Elsevier Ltd


  • Cloning
  • Cold-active
  • Lipase
  • Pichia lynferdii

ASJC Scopus subject areas

  • Biotechnology
  • Food Science
  • Bioengineering
  • Applied Microbiology and Biotechnology
  • Agronomy and Crop Science


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