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Effect of Candida antarctica Lipase B Immobilization on the Porous Structure of the Carrier
Author(s) -
Miletić Nemanja,
Vuković Zorica,
Nastasović Aleksandra,
Loos Katja
Publication year - 2011
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.201100127
Subject(s) - candida antarctica , lipase , glutaraldehyde , hydrolysis , porosity , chemistry , porosimetry , copolymer , specific surface area , particle size , immobilized enzyme , polymer chemistry , chemical engineering , chromatography , organic chemistry , enzyme , polymer , porous medium , catalysis , engineering
A series of poly(GMA ‐co‐ EGDMA) resins with identical composition but varying particle sizes, pore radii, specific surface areas and specific volumes are studied to assess how Candida antarctica lipase B immobilization affects the porosity of the copolymer particles. Mercury porosimetry reveals a significant change in the average pore size (up to 6.1‐fold), the specific surface area (up to 3.2‐fold) and the specific volume (up to 2.1‐fold) of the epoxy resin. A similar behaviour is observed for glutaraldehyde‐modified epoxy resins. The influences of the resin porosity properties on the loading of Candida antarctica lipase B during immobilization and on the hydrolytic activity (hydrolysis of p ‐nitrophenyl acetate) of the immobilized lipase are studied.