Purification and characterization of a cold-active lipase from Pichia lynferdii Y-7723: pH-dependant activity deviation

Jae Han Bae, Mi Hyun Kwon, In-Hwan Kim, Ching T. Hou, Hak Ryul Kim

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7 Citations (Scopus)


Lipases with abnormal functionalities such as high thermostability and optimal activity at extreme conditions gain special attentions because of their applicability in the restricted reaction conditions. In particular, coldactive lipases have gained special attentions in various industrial fields such as washer detergent, pharmaceutical catalyst, and production of structured lipid. However, production of cold-active lipase is mostly found from psychrophilic microorganisms. Recently we found a novel cold-active lipase from Pichia lynferdii Y-7723 which is mesophilic yeast strain. In this study, we purified the cold active lipase and the enzyme was further characterized in several parameters. The enzyme was purified with 33 purification fold using chromatographic techniques and the purified lipase represented maximum lipolytic activity at 15°C and the maximum activity was highly dependent on pH.

Original languageEnglish
Pages (from-to)851-857
Number of pages7
JournalBiotechnology and Bioprocess Engineering
Issue number5
Publication statusPublished - 2014 Jan 1



  • characterization
  • cold-active
  • lipase
  • pH-dependency
  • Pichia lynferdii

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Biomedical Engineering
  • Bioengineering

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