Solid-phase modification with succinic polyethyleneglycol of aminated lipase B from Candida antarctica: Effect of the immobilization protocol on enzyme catalytic properties

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

“…It is possible to observe the great variety of materials used for lipase immobilization. Among the hydrophobic materials used, it is possible to find functionalized bentonites including both acid activated bentonite and organically modified bentonite with cetyltrimethyl ammonium bromide (Dong et al, 2013), octyl-Sepharose (Almeida et al, 2018Barbosa et al, 2012b;Galvis et al, 2012;Ghattas et al, 2014;Habibi et al, 2013;Kurtovic et al, 2011;Manoel et al, 2015a;Ruiz et al, 2013;Volpato et al, 2011), Lewatit VP OC 1600 (a macroporous acrylic polymer resin) (Kurtovic et al, 2011), magnetic microspheres with carboxyl groups prepared by copolymerization of vinyl acetate, acrylamide, and acrylic acid (Zhang et al, 2012), hydrophobic silk fibers functionalized with methyl groups (Chen et al, 2012), sol-gel materials based on n-propyltrimethoxysilane/tetraethoxysilane (Hu et al, 2013), hydrophobic magnetic particles functionalized with the organosilane surfactant [3-(trimethoxysilyl) propyl] octadecyldimethylammonium chloride , D4020, a nonpolar hydrophobic resin (Liu et al, 2013), a NKA macroporous resin (polystyrene) (Liu et al, 2011;Su et al, 2014), nonwoven viscose fabric coated with methyl groups through treatment with polydimethyliloxane (Weina Li et al, 2011), Sepabeads (macroporous acrylic support) activated with octadecyl groups (Hernandez et al, 2011b), silica aerogels modified with methyl groups (Gao et al, 2010), D152H (macroporous resin, acreylic-divinylbenzene) (Yan et al, 2013), small or large poly-hydroxybutyrate beads (Mendes et al, 2012), porous magnetic polymeric microspheres based on poly(methylmethacrylate-co-divinylbenzene)-Fe 3 O 4 (Meng et al, 2013), octyl-agarose cross-linked with dextran sulfate (Pizarro et al, 2012), polyacrylonitrile nanofibers membrane (Gupta et al, 2013), MSU-H (Michigan State University) type mesoporous (Yu et al, 2013), mesoporous silica with same pore size but with varying particle size (Gustafsson et al, 2012), styrene-divinylbenzene MCI GEL CHP20P porous support (de Abreu et al, 2014;Martins et al, 2013;Poppe et al, 2013), Diaion HP20LX (p...…”

Stabilization of Immobilized Lipases by Intense Intramolecular Cross-Linking of Their Surfaces by Using Aldehyde-Dextran Polymers

“…One gram of conjugate was incubated in 1 M ethylenediamine pH 4.75 at 25 °C, containing different concentrations (10, 4, or 1 mM) of soluble carbodiimide 1-ethyl-3-[3-dimethylaminopropil] carbodiimide (EDAC) [ 44 , 45 , 46 ]. One-hundred percent of the carboxyl groups were modified with 10 mM carbodiimide, 80% were modified with 4 mM carbodiimide and 50% were modified with 1 mM carbodiimide [ 35 , 47 ]. After 1.5 h at room temperature under gentle stirring, the conjugate was filtered and washed with a 25 mM sodium phosphate buffer pH 7.0.…”

Chemical Modification in the Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities

“…This polymer may impose some steric hindrance on the movements of enzyme chains, for example, PEI has been used to maintain the open form of a phospholipase induced by detergents 46. Chemical modification with polyethyleneglycol is usually utilized to hydrophobize enzyme surfaces and this improves enzyme solubility in organic media and may also be used to tune the properties of the enzyme 45…”

“…These approaches have reached more sophisticated strategies, in which the immobilized enzyme is previously chemically modified to improve the reactivity of the protein surface. Thus, lipase B from C. antarctica (CALB) has been modified using succinic polyethyleneglycol through the carbodiimide route after amination of the modified enzyme surface 45. Modification of immobilized (on octyl agarose and Eupergit C) CALB native amino groups did not produce a significant alteration of amino groups in CALB, whereas, after preliminary chemical amination, around 14–15 PEG molecules could be introduced per enzyme molecule.…”

“…Modification of immobilized (on octyl agarose and Eupergit C) CALB native amino groups did not produce a significant alteration of amino groups in CALB, whereas, after preliminary chemical amination, around 14–15 PEG molecules could be introduced per enzyme molecule. Again, the effect on the functional properties of the modifications depended on the immobilization protocol and substrate 45. Chemical modification may be directed to have a carrier protein coated with an interesting molecule, for example, to induce an immunogenic response or to prepare chimeric proteins.…”