Kinetic properties of soluble and immobilized Candida rugosa lipase

Mar'ia D. Virto, ISabel Agud, Sol Montero, Alicia Blanco, Rodolfo Solozabal, Jos'e M. Lascaray, Mar'ia J. Llama, Juan L. Serra, L. Carlos Landeta*, Mertxe De Renobales

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

Immobilized lipase (triacylglycerol ester hydrolase, EC 3.1.1.3) from Candida rugosa has been immobilized on commercially available microporous polypropylene and used for the batch hydrolysis of different animal fats. The effect of the reaction products at concentrations similar to those obtained at 90% hydrolysis, both on soluble and immobilized lipase, was studied. Glycerol showed low inhibitory effect but oleic acid caused 50% inhibition. A mixture of free fatty acids present in the complete hydrolysis of beef tallow inhibited lipase activity more than 70%. The stability of the enzyme (both soluble and immobilized) was highest in the presence of 20% isooctane. The apparent Michaelis constant for each substrate for the soluble enzyme did not change on immobilization.

Original languageEnglish
Pages (from-to)127-136
Number of pages10
JournalApplied Biochemistry and Biotechnology
Volume50
Issue number2
DOIs
Publication statusPublished - Feb 1995

Keywords

  • animal fats hydrolysis
  • Candida rugosa
  • EC 3.1.1.3
  • immobilized enzyme
  • kinetic parameters
  • Lipase
  • organic solvents

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