Effects of non-covalent interaction of dimethyl suberimidate on lipase stability

Masaya Kawase, Kenji Sonomoto, Atsuo Tanaka

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2 Citations (Scopus)


The hydrolytic activity of the purified yeast lipase OF 360 was greatly decreased by heating above 45°C and the residual activity after heating at 50°C for 15 min was about one-tenth of the original. Treatment of the lipase with a Afunctional reagent, dimethyl suberimidate (DMS), increased the heat stability. Stabilization by DMS treatment was supposed to be caused by non-covalent interaction between the lipase and DMS through electrostatic and/or hydrophobic forces. In addition, analysis of FT-IR spectra of the DMS- and non-treated lipases suggested that the main skeleton of the treated lipase was little perturbed by heating.

Original languageEnglish
Pages (from-to)2605-2609
Number of pages5
JournalAgricultural and Biological Chemistry
Issue number10
Publication statusPublished - Jan 1 1990
Externally publishedYes


All Science Journal Classification (ASJC) codes

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)

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