Assessment of two immobilized lipases activity and stability to low temperatures in organic solvents under ultrasound-assisted irradiation

Bioprocess Biosyst Eng. 2012 Mar;35(3):351-8. doi: 10.1007/s00449-011-0573-4. Epub 2011 Jul 22.

Abstract

Both stability and catalytic activity of two commercial immobilized lipases were investigated in the presence of different organic solvents in ultrasound-assisted system. In a general way, for Novozym 435, the use of ethanol as solvent led to a loss of activity of 35% after 10 h of contact. The use of iso-octane conducted to a gradual increase in lipase activity in relation to the contact time, reaching a maximum value of relative activity of 126%. For Lipozyme RM IM, after 5 h of exposure, the enzyme presented no residual activity when ethanol was used as solvent. The solvents tert-butanol and iso-octane showed an enhancement of about 20 and 17% in the enzyme activity in 6 h of exposure, respectively. Novozym 435 and Lipozyme IM presented high stability to storage after treatment under ultrasound-assisted system using n-hexane and tert-butanol as solvents.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzymes, Immobilized / chemistry*
  • Fungal Proteins
  • Lipase / chemistry*
  • Octanes / chemistry*
  • Solvents / chemistry*
  • Sound*
  • Temperature
  • Time Factors

Substances

  • Enzymes, Immobilized
  • Fungal Proteins
  • Octanes
  • Solvents
  • Lipozyme
  • Novozyme 435
  • Lipase
  • 2,2,4-trimethylpentane