Immobilization and characterization of porcine pancreas lipase

K. Bagi, L. M. Simon, B. Szajáni

Research output: Contribution to journalArticle

75 Citations (Scopus)

Abstract

Porcine pancreas lipase (triacylglycerol ester hydrolase, EC 3.1.1.3) was immobilized with the highest activity (2,187 U g-1 solid) on polyacrylamide beads possessing carboxylic functional groups activated by a water-soluble carbodiimide. The optimum pH for catalytic activity was pH 8.9. The apparent optimum temperature for the immobibized enzyme was about 7°C higher than that for the soluble enzyme. The immobilization stabilized the enzyme against heat and urea treatment. Cross-linking of the immobilized enzyme with glutaraldehyde or 3,5-difluoronitrobenzene improved the thermal stability. Application of the immobilized lipase for olive oil hydrolysis is also presented.

Original languageEnglish
Pages (from-to)531-535
Number of pages5
JournalEnzyme and Microbial Technology
Volume20
Issue number7
DOIs
Publication statusPublished - May 28 1997

Keywords

  • Conformational stability
  • Cross-linking
  • Immobilization
  • Porcine pancreas lipase

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

Fingerprint Dive into the research topics of 'Immobilization and characterization of porcine pancreas lipase'. Together they form a unique fingerprint.

  • Cite this