Evaluation of cellulose-binding domain fused to a lipase for the lipase immobilization

Sangpill Hwang, Jungoh Ahn, Sumin Lee, Tai Gyu Lee, Seungjoo Haam, Kangtaek Lee, Ik Sung Ahn, Joon Ki Jung

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35 Citations (Scopus)


A cellulose-binding domain (CBD) fragment of a cellulase gene of Trichoderma hazianum was fused to a lipase gene of Bacillus stearothermophilus L1 to make a gene cluster for CBD-BSL lipase. The specific activity of CBD-BSL lipase for oil hydrolysis increased by 33% after being immobilized on Avicel (microcrystalline cellulose), whereas those of CBD-BSL lipase and BSL lipase decreased by 16% and 54%, respectively, after being immobilized on silica gel. Although the loss of activity of an enzyme immobilized by adsorption has been reported previously, the loss of activity of the CBD-BSL lipase immobilized on Avicel was less than 3% after 12 h due to the irreversible binding of CBD to Avicel.

Original languageEnglish
Pages (from-to)603-605
Number of pages3
JournalBiotechnology Letters
Issue number7
Publication statusPublished - 2004 Apr

Bibliographical note

Funding Information:
This work was made possible with funding provided by the Korea Science & Engineering Foundation to Advanced Environmental Biotechnology Research Center at POSTECH.

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


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