Purification and characterization of extracellular lipase from Acinetobacter radioresistens CMC-2

I-Son Ng, Shau Wei Tsai, Shu Jen Chen

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6 Citations (Scopus)


A novel lipase with the favorable alkaline and thermostable characteristics was produced from Acinetobacter radioresistens CMC-2. The crude lipase with 49.5% of total activity was recovered after centrifugation, ultrafiltration and lyophilization. The crude preparation was further purified to a homogeneous state by column chromatography on phenyl sepharose and ultrafiltration, giving 26.6% of total activity recovery. The molecular weight and isoelectric point of the lipase determined by SDS-PAGE and IEF were 38 kDa and 4.5, respectively. The lipase could be classified as a 1,3-positional specific enzyme and possessed the (R)-stereoselectivity in the hydrolysis of racemic suprofen trifluoroethyl ester in isooctane. Moreover, effects of pH, temperature, metal ions, surfactants and organic solvents on the enzyme activity and stability were reported.

Original languageEnglish
Pages (from-to)355-362
Number of pages8
JournalJournal of the Chinese Institute of Chemical Engineers
Issue number5
Publication statusPublished - 1999 Sept 1

All Science Journal Classification (ASJC) codes

  • General Chemistry
  • General Chemical Engineering


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