Pure silica zeolites have been prepared in powder and pellets form with different surface chemical properties in order to investigate how the binding forces in the lipase enzyme adsorption influence the final conformation of the immobilized enzyme and its catalytic activity. The catalytic activity of the adsorbed lipase have been tested in the alkyl esters hydrolysis reaction. The higher alkyl-esters conversion is observed for the lipase immobilized on the supports prepared in OH- media compared to the fluoride media supports. The obtained results can be explained by the two different non-covalent interactions between the external surface of zeolites and the enzyme
Lipases, also known as glycerol ester hydrolases , are enzymes that belong to the group of serine hy...
Enzymes exhibit high selectivity and reactivity under normal conditions but are sensitive to denatur...
A novel method to prepare immobilized lipases derivatives is hereby proposed. Lipases are firstly ad...
Pure silica zeolites have been prepared in powder and pellets form with different surface chemical ...
Immobilization of Lipase from Rhizomucor miehei on Silicalite-1 self-bonded pellets prepared by F a...
none7In this paper the performance of different supports respect to the lipase immobilization was in...
In order to understand the role of the acidbase, electrostatic and covalent interactions between enz...
none5Enzymes have important catalytic properties: high specificity, high enantio- and regio-selectiv...
In this paper, the preparation and characterization of the Rhizomucor miehei Lipase/zeolite catalyst...
Immobilization of Pseudomonas fluorescens lipase (Pfl) on the chemically modified, or unmodified, su...
Three mesoporous materials, silica, alumina and titania, were used as host for a lipase and the enzy...
Lipase from Candida rugosa was immobilized by adsorption onto laboratory prepared supports, silica S...
Hydrophobic wrinkled silica nanoparticles (WSNs) were obtained by surface functionalization with per...
Lipase (EC 3.1.1.3) is a tri-acylglycerol ester hydrolase, catalysing the hydrolysis of tri-, di-, a...
Lipases are ubiquitous enzymes whose physiological role is the hydrolysis of triacylglycerol into fa...
Lipases, also known as glycerol ester hydrolases , are enzymes that belong to the group of serine hy...
Enzymes exhibit high selectivity and reactivity under normal conditions but are sensitive to denatur...
A novel method to prepare immobilized lipases derivatives is hereby proposed. Lipases are firstly ad...
Pure silica zeolites have been prepared in powder and pellets form with different surface chemical ...
Immobilization of Lipase from Rhizomucor miehei on Silicalite-1 self-bonded pellets prepared by F a...
none7In this paper the performance of different supports respect to the lipase immobilization was in...
In order to understand the role of the acidbase, electrostatic and covalent interactions between enz...
none5Enzymes have important catalytic properties: high specificity, high enantio- and regio-selectiv...
In this paper, the preparation and characterization of the Rhizomucor miehei Lipase/zeolite catalyst...
Immobilization of Pseudomonas fluorescens lipase (Pfl) on the chemically modified, or unmodified, su...
Three mesoporous materials, silica, alumina and titania, were used as host for a lipase and the enzy...
Lipase from Candida rugosa was immobilized by adsorption onto laboratory prepared supports, silica S...
Hydrophobic wrinkled silica nanoparticles (WSNs) were obtained by surface functionalization with per...
Lipase (EC 3.1.1.3) is a tri-acylglycerol ester hydrolase, catalysing the hydrolysis of tri-, di-, a...
Lipases are ubiquitous enzymes whose physiological role is the hydrolysis of triacylglycerol into fa...
Lipases, also known as glycerol ester hydrolases , are enzymes that belong to the group of serine hy...
Enzymes exhibit high selectivity and reactivity under normal conditions but are sensitive to denatur...
A novel method to prepare immobilized lipases derivatives is hereby proposed. Lipases are firstly ad...