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    Lipase immobilisation on magnetic silica nanocomposite particles: Effects of the silica structure on properties of the immobilised enzyme

    , Article Journal of Materials Chemistry ; Volume 22, Issue 17 , 2012 , Pages 8385-8393 ; 09599428 (ISSN) Kalantari, M ; Kazemeini, M ; Tabandeh, F ; Arpanaei, A ; Sharif University of Technology
    2012
    Abstract
    Uniformly sized superparamagnetic single-shell nonporous (S1) and double-shell mesoporous silica nanocomposite particles with ∼130 nm magnetite cluster cores are synthesised in this study. Mesoporous particles are prepared with two BJH pore sizes (2.44 and 3.76 nm, designated as S2 and S3 particles, respectively). Once the lipase was immobilised on particles, our results showed that the enzyme loading capacities of mesoporous structures, i.e. S2 and S3, are higher than that for nonporous particles (S1). Hydrolytic activity tests reveal that immobilised lipases retain about 90% of the free enzyme's activity. Furthermore, comparing to the free enzyme, the thermal stability of immobilised... 

    Immobilization of penicillin G acylase on non-porous ultrafine silica particles

    , Article Scientia Iranica ; Volume 12, Issue 3 , 2005 , Pages 295-299 ; 10263098 (ISSN) Fazelinia, H ; Kheirolomoom, A ; Sharif University of Technology
    Sharif University of Technology  2005
    Abstract
    In this paper, immobilization of penicillin G aclylase onto non-porous ultrafine silica particles has been studied. The amount of penicillin G acylase immobilized was increased by increasing the free enzyme concentration and, at 0.45 mg/ml concentration of the free enzyme, 80% of the enzyme was immobilized. The optimum pH for immobilization was found to be 7.0, close to the pl of the enzyme. Although immobilization of the enzyme on ultrafine silica particles with and without glutaraldehyde showed almost the same activities, the enzyme immobilized with glutaraldehyde retained its initial activity much longer during 40 cycle-repeated batches with a half life of 163.2 h. © Sharif University of... 

    Phenols removal by immobilized horseradish peroxidase

    , Article Journal of Hazardous Materials ; Volume 166, Issue 2-3 , 2009 , Pages 1082-1086 ; 03043894 (ISSN) Alemzadeh, I ; Nejati, S ; Sharif University of Technology
    2009
    Abstract
    Application of immobilized horseradish peroxidase (HRP) in porous calcium alginate (ca-alginate) for the purpose of phenol removal is reported. The optimal conditions for immobilization of HRP in ca-alginate were identified. Gelation (encapsulation) was optimized at 1.0% (w/v) sodium alginate in the presence of 5.5% (w/v) of calcium chloride. Upon immobilization, pH profile of enzyme activity changes as it shows higher value at basic and acidic solution. Increasing initial phenol concentration results in a decrease in % conversion. The highest conversion belongs to phenol concentration of 2 mM. Investigation into time course of phenol removal for both encapsulated and free enzymes showed...