2016
DOI: 10.21577/0103-5053.20160319
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Physical-Chemical Properties of the Support Immobead 150 Before and After the Immobilization Process of Lipase

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Cited by 11 publications
(12 citation statements)
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References 31 publications
(48 reference statements)
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“…As time passed, it became tougher to occupy the available vacant surface sites due to the repelling forces amongst the solute molecules that occurred in the solid and bulk phases [32]. This was implicated by the reduction of the pore size of the carrier by way of increasing the original protein loading, which significantly constrained the diffusion of enzyme molecules to its interior side [33]. Therefore, it was anticipated that these aggregates would be multiplied at the high enzyme concentration, which would lead to a lower rate of diffusion to the carrier microenvironment [15].…”
Section: Adsorption Kinetics Studiesmentioning
confidence: 99%
“…As time passed, it became tougher to occupy the available vacant surface sites due to the repelling forces amongst the solute molecules that occurred in the solid and bulk phases [32]. This was implicated by the reduction of the pore size of the carrier by way of increasing the original protein loading, which significantly constrained the diffusion of enzyme molecules to its interior side [33]. Therefore, it was anticipated that these aggregates would be multiplied at the high enzyme concentration, which would lead to a lower rate of diffusion to the carrier microenvironment [15].…”
Section: Adsorption Kinetics Studiesmentioning
confidence: 99%
“…Nitrogen physisorption studies have revealed that, the pore volume of thiol modified CO-MTS materials decreases from 1.0336 cm 3 /g before immobilization to 0.8169 cm 3 /g after trypsin immobilization [32]. The decrease in pore volume after enzyme immobilization is not strange and is due to coating of the support surface by the enzyme molecule [40].…”
Section: Immobilization Of Trypsin Enzymes On Co-mts Via Thiol-disulfmentioning
confidence: 99%
“…e results obtained by HPTLC showed that CAL-Bo showed no catalytic activity in any of the combinations of organic solvents, possibly due to the immobilisation support to which the enzyme was attached. Lipase Candida CAL-Bo is immobilised in support Immobead 150, which is formed of methacrylate copolymers with epoxy functions, with an average particle size of 150-300 μm and presents a wide pore size range, with pores in the micropore and mesopore region [30]. In contrast, CAL-Bn is immobilised on a macroporous acrylic poly resin (methyl methacrylate-co-divinylbenzene), having an average particle size of 315-1000 μm and a pore diameter of ∼150Å [31,32].…”
Section: Enzymatic Transesterification Reaction Undermentioning
confidence: 99%
“…In contrast, CAL-Bn is immobilised on a macroporous acrylic poly resin (methyl methacrylate-co-divinylbenzene), having an average particle size of 315-1000 μm and a pore diameter of ∼150Å [31,32]. Both supports show hydrophobic properties; however, the pore size of the enzyme CAL-Bo (12-20Å) is smaller than that of CAL-Bn (∼150Å) and the pore size distribution is not homogeneous [30]. is characteristic is determinant for the enzyme-substrate coupling; a small pore size or inhomogeneous pore size allows only the smallest substrates to penetrate.…”
Section: Enzymatic Transesterification Reaction Undermentioning
confidence: 99%