Immobilization and characterization of porcine pancreas lipase

K. Bagi, L. M. Simon, B. Szajáni

Research output: Contribution to journalArticle

74 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 - 1997

Fingerprint

Lipases
Lipase
Immobilization
Pancreas
Swine
Enzymes
Hot Temperature
Carbodiimides
Immobilized Enzymes
Glutaral
Hydrolases
Olive oil
Functional groups
Urea
Hydrolysis
Catalyst activity
Esters
Thermodynamic stability
Polyacrylates
Temperature

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this

Immobilization and characterization of porcine pancreas lipase. / Bagi, K.; Simon, L. M.; Szajáni, B.

In: Enzyme and Microbial Technology, Vol. 20, No. 7, 1997, p. 531-535.

Research output: Contribution to journalArticle

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