A method for lipase co-precipitation in a biodegradable protein matrix

M. Golubovic, S. H. Van Hateren, M. Ottens*, G. J. Witkamp, L. A.M. Van Der Wielen

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


This article presents a novel method for immobilization of active ingredients. The method is based on CO2 aided active ingredient co-precipitation with glycinin, a biodegradable protein matrix from edible soybean protein. Glycinin precipitates abundantly under isoelectric conditions and serves as the matrix within which the active substance is trapped during the precipitation process. The enzyme lipase from Candida rugosa was successfully co-precipitated into the protein pellet to prove the principle. It was shown that the lipase within the co-precipitate retained lipase and esterase activity under different pH conditions. In some cases the activity was even higher than the activity of crude lipase, possibly due to the protective role of the matrix protein. Due to the retained lipase activity and food-grade quality of the binary precipitate, it has potential of being used in the food or pharmaceutical industry. Additional quality of the binary precipitate is the potentially significantly reduced downstream processing due to the fact that no organic solvents or precipitants were used in the precipitation process.

Original languageEnglish (US)
Pages (from-to)1209-1218
Number of pages10
JournalBiotechnology and Bioengineering
Issue number6
StatePublished - Dec 15 2007
Externally publishedYes


  • Binary precipitate
  • Glycinin
  • Immobilization
  • Isoelectric precipitation
  • Lipase
  • Protein-protein co-precipitation
  • Protein-protein interaction

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


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