Activity enhancement and stabilization of lipase from Pseudomonas cepacia in polyallylamine-mediated biomimetic silica

Biotechnol Lett. 2011 Mar;33(3):525-9. doi: 10.1007/s10529-010-0451-1. Epub 2010 Nov 3.

Abstract

Triacylglycerol lipase from Pseudomonas cepacia and Fe(3)O(4) magnetic nanoparticles were encapsulated simultaneously within biomimetic silica through the catalysis of polyallylamine. The encapsulation efficiency reached 96% with an activity recovery of 51%. After 5 h at 37°C, the activities of the free and encapsulated lipases decreased by 77 and 16%, respectively. Addition of 10 and 15 mol% trimethylmethoxysilane to tetramethoxysilane during encapsulation doubled the lipase activity while inclusion of 50 and 60 mol% γ-(methacryloxypropyl)-trimethoxysilane tripled the activity. Thus, such encapsulation not only stabilized P. cepacia lipase but also could enhance the activity by varying silane additives.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biomimetics
  • Burkholderia cepacia / enzymology*
  • Enzyme Activation
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Lipase / chemistry
  • Lipase / metabolism*
  • Polyamines / chemistry*
  • Silicon Dioxide / chemistry*
  • Temperature

Substances

  • Polyamines
  • polyallylamine
  • Silicon Dioxide
  • Lipase