Immobilization of lipase from Mucor miehei and Rhizopus oryzae into mesoporous silica - The effect of varied particle size and morphology
Artikel i vetenskaplig tidskrift, 2012

Immobilization of enzymes usually improves the recyclability and stability and can sometimes also improve the activity compared to enzymes free in solution. Mesoporous silica is a widely studied material as host for immobilized enzymes because of its large internal surface area and tunable pores. It has previously been shown that the pore size is critical both for the loading capacity and for the enzymatic activity; however, less focus has been given to the influence of the particle size. In this work the effect of particle size and particle morphology on the immobilization of lipase from Mucor miehei and Rhizopus oryzae have been investigated. Three kinds of mesoporous silica, all with 9 nm pores but with varying particle size (1000 nm, 300 nm and 40 nm) have been synthesized and were used as host for the lipases. The two lipases, which have the same molecular size but widely different isoelectric points, were immobilized into the silica particles at varied pH values within the interval 5 to 8. The 300 nm particles were proven to be the most suitable carrier with respect to specific activity for both enzymes. The lipase from Mucor miehei was more than four times as active when immobilized at pH 8 compared to free in solution whereas the difference was less pronounced for the Rhizopus oryzae lipase.

biocatalysis

particle morphology

lipase

immobilization

Mesoporous silica

enzymes

Författare

Hanna Gustafsson

Chalmers, Kemi- och bioteknik, Teknisk ytkemi

SuMo Biomaterials

Emma Johansson

Linköpings universitet

Albert Barrabino Ponce

Chalmers, Kemi- och bioteknik

M. Oden

Linköpings universitet

Krister Holmberg

Chalmers, Kemi- och bioteknik, Teknisk ytkemi

Colloids and Surfaces B: Biointerfaces

0927-7765 (ISSN)

Vol. 100 22-30

Styrkeområden

Nanovetenskap och nanoteknik

Livsvetenskaper och teknik

Materialvetenskap

Ämneskategorier

Fysikalisk kemi

Biokemi och molekylärbiologi

Annan kemiteknik

DOI

10.1016/j.colsurfb.2012.04.042

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Senast uppdaterat

2018-02-28