Trypsin immobilization on mesoporous silica with or without thiol functionalization

Jang, Soo-Hyun; Kim, Dong‐Jun; Choi, Jungsik; Row, Kyung‐Ho; Ahn, Wha‐Seung

doi:10.1007/s10934-006-8035-0

Cited by 33 publications

(17 citation statements)

References 23 publications

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“…But as Ackerman et al [15,19] pointed out most recently, that performance can further be improved if functionalised (aminated or carboxylated) mesoporous silica (FMS) with even larger pores are applied as enzyme carriers. This suggests further studies of the use of either large pore SBA-15 materials, applied in [15,19], or cellular foams of the MCF type, also strongly recommended by several groups [9,[21][22][23][24][25] as the supports of choice for a variety of enzymes.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Invertase on Mesoporous Silicas to Obtain Hyper Active Biocatalysts

2009

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Comparative studies of invertase immobilized on two mesoporous cellular foams (MCF) and two supports of SBA-15 type with different pore sizes, using three highly recommended methods of protein bonding showed that activity of aminated MCF-based biocatalysts is significantly higher than that of SBA-15 counterparts, with the same textural properties. Specific activities of invertase covalently attached via GLA spacer was about 73-111% of a native enzyme. A unique microenvironment of functionalized cage-like pores of aminated MCFs is deemed to be responsible for this ultra high activity of invertase.

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Section: Introductionmentioning

confidence: 99%

Immobilization of Invertase on Mesoporous Silicas to Obtain Hyper Active Biocatalysts

2009

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“…Next to traditional ceramics, several other systems with high specific surface area and porosity, that are able to deliver molecules with therapeutic activity, have already been investigated, such as phosphates, glasses, bone cements and silica sol-gel materials. The possibility to modulate mesopore size also allows one to adsorb larger molecules than ibuprofen, such as antibiotics, [16][17][18] enzymes 19,20 and, in general, proteins. Since the first use of MCM-41 for ibuprofen delivery, 7 the role of the pore diameter, the influence of functional groups, 8-13 the particle morphology and the pore geometry 14,15 have been investigated.…”

Section: Introductionmentioning

confidence: 99%

“…25 By varying the alumina membrane nanochannel diameter from 18 to 80 nm, different channel structures of the silica-surfactant mesophases were observed, in a progression starting from spheres, to straight cylinders, to concentric inner shells. 26 Thus OMS inside AAMs having mesopores with a columnar or circular structure and different pore diameters were obtained using different surfactants such as n-hexadecyltrimethylammonium bromide (CTAB) or triblock copolymer [Pluronic P123, (EO 20 PO 70 EO 20 )]. 26 Thus OMS inside AAMs having mesopores with a columnar or circular structure and different pore diameters were obtained using different surfactants such as n-hexadecyltrimethylammonium bromide (CTAB) or triblock copolymer [Pluronic P123, (EO 20 PO 70 EO 20 )].…”

Section: Introductionmentioning

confidence: 99%

Large antibiotic molecule diffusion in confined mesoporous silica with controlled morphology

et al. 2008

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“…14-16 BAPNA is frequently used as a substrate for free or immobilized trypsin. [14][15][16] The reaction between trypsin and BAPNA is shown in Figure 3.…”

Section: Measurement Of Relative Activitymentioning

confidence: 99%

Development of an enzyme-immobilized support using a polyester woven fabric

Shim

Lee

Song

et al. 2016

Textile Research Journal

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In this study, we aimed to develop an enzyme-immobilized support using polyester woven fabrics and to optimize the development process. We obtained information about the storage stability and reusability of the enzyme and showed the applicability of the polyester woven fabric as an enzyme-immobilized support. In particular, the samples hydrolyzed by hydrogen chloride were treated with N,N'-dicyclohexylcarbodiimide and N-hydroxysuccinimide to activate the surfaces. We evaluated the relative activity of the enzyme immobilization processes, the introduction of spacers, crosslinking and enzyme immobilization and optimized these parameters. The introduction process was controlled to a bovine serum albumin concentration of 1.5% (w/v) and treatment time of 3 h. The crosslinking process was optimized to pH 10.0, a glutaraldehyde concentration of 3% (v/v) and a crosslinking time of 90 min. The immobilization conditions were maintained at pH 8.5, a temperature of 25 C, a time of 45 min and a trypsin concentration of 6% (o.w.f.).Enzyme-immobilized supports have been used in various medical applications, food production processes, ion batteries and filters for waste-water purification. 1,2 Numerous methods for enzyme immobilization on different supports have been described in the literature. Ideal support properties include mechanical stability, hydrophilicity, resistance to microbial attack, porosity and availability at low cost. 2,3 The application of fabrics as immobilization supports could offer several advantages in terms of price and structure compared with other materials such as gels, beads, membranes and films. 2-4 Fabrics are commercially available and relatively cheaper than these or inorganic materials. The fiber-based structures have a high porosity and a large average pore size, so that more enzymes are immobilized, and the immobilized enzymes are protected from the environment. [2][3][4] There are various fabric supports available for enzyme immobilization, which can be classified into natural and synthetic fibers. Natural fibers such as cellulose and chitosan, which have excellent biocompatibility and hydrophilicity, are non-toxic and biodegradable. However, the weak mechanical stability of these natural fibers has greatly limited their application. 3,5 Synthetic fibers such as polylactic acid, polystyrene, polyamide and polyester (polyethylene terephthalate, PET) can be used for enzyme supports due to their good mechanical stability. However, their hydrophobicity is the major disadvantage. It is well known that the hydrophobic interaction between the enzyme and the support is one of the main reasons for protein denaturation. 3,5 One method to address these problems is to introduce spacers between the enzymes and the support. 6 This is a common method to reduce undesirable interactions between the functional groups of support surfaces and the enzyme molecule, and to lower steric hindrance. 7 In particular, the introduction of spacers increases the distance between the enzyme and the hydrophobic surfaces of sy...

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Trypsin immobilization on mesoporous silica with or without thiol functionalization

Cited by 33 publications

References 23 publications

Immobilization of Invertase on Mesoporous Silicas to Obtain Hyper Active Biocatalysts

Immobilization of Invertase on Mesoporous Silicas to Obtain Hyper Active Biocatalysts

Large antibiotic molecule diffusion in confined mesoporous silica with controlled morphology

Development of an enzyme-immobilized support using a polyester woven fabric

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