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Immobilization ofCandida rugosalipase on sporopollenin fromLycopodium clavatum

Authors
Journal
International Journal of Biological Macromolecules
0141-8130
Publisher
Elsevier
Publication Date
Volume
45
Issue
3
Identifiers
DOI: 10.1016/j.ijbiomac.2009.06.014
Keywords
  • Sporopollenin
  • Physical Adsorption
  • Lycopodium Clavatum
  • Immobilization
  • Lipase
Disciplines
  • Biology
  • Chemistry

Abstract

Abstract Sporopollenin is a natural polymer obtained from Lycopodium clavatum, which is highly stable with constant chemical structure and has high resistant capacity to chemical attack. In this study, immobilization of lipase from Candida rugosa (CRL) on sporopollenin by adsorption method is reported for the first time. Besides this, the enzyme adsorption capacity, activity and thermal stability of immobilized enzyme have also been investigated. It has been observed that under the optimum conditions (Spo-E (0.3)), the specific activity of the immobilized lipase on the sporopollenin by adsorption was 16.3 U/mg protein, which is 0.46 times less than that of the free lipase (35.6 U/mg protein). The pH and temperature of immobilized enzyme were optimized, which were 6.0 and 40 °C respectively. Kinetic parameters V max and K m were also determined for the immobilized lipase. It was observed that there is an increase of the K m value (7.54 mM) and a decrease of the V max value (145.0 U/mg-protein) comparing with that of the free lipase.

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