Can lipases hydrolyze a peptide bond?

Tatsuo Maruyama, Mitsutoshi Nakajima, Hidemasa Kondo, Kosei Kawasaki, Minoru Seki, Masahiro Goto

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)

Abstract

Several research groups reported that lipase catalyzes peptide synthesis in organic solvents. Structural studies revealed that the catalytic triad of lipase consists of Ser, His, and Asp, the same as serine proteases. Lipase has a potential to have peptidase activity. In this report, we investigated the peptidase activity of lipases. Of 13 lipases of diverse origin tested, only commercially available porcine pancreatic lipase (PPL) exhibited peptidase activity. However, purification of PPL by gel permeation chromatography separated the peptidase and lipolytic activities of PPL. This study clearly demonstrated that all the lipases tested do not hydrolyze a peptide bond.

Original languageEnglish
Pages (from-to)655-657
Number of pages3
JournalEnzyme and Microbial Technology
Volume32
Issue number6
DOIs
Publication statusPublished - May 20 2003

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

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