Improving Adsorbent Properties of Cage-like Ordered Amine Functionalized Mesoporous Silica with Very Large Pores for Bioadsorption

Hartono, Sandy Budi; Qiao, Shi Zhang; Jack, Kevin S.; Ladewig, Bradley P.; Hao, Zhengping; Lu, Gao Qing

doi:10.1021/la900023p

Cited by 137 publications

(85 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4 One approach to increase the performance of the enzymatic process is to immobilize the enzymes in/on solid supports which renders them reusable and hence reduces the enzyme-related operating costs. 5 The past decade saw a large variety of mesoporous silicas being tested for their enzyme immobilization efficiency, [6][7][8][9][10][11][12] since they displayed many characteristics that may be beneficial for such a purpose, i.e., high surface area, narrow pore size distribution, tunable pore size, and high chemical and mechanical stability. [13][14][15][16] However, due to size exclusion effects occurring at the pore entries, most of these studies were limited to small proteins and enzymes.…”

Section: Introductionmentioning

confidence: 99%

Functionalized Mesoporous Silica with Very Large Pores for Cellulase Immobilization

et al. 2010

Self Cite

View full text Add to dashboard Cite

Organo-functionalized FDU-12 type silicas exhibiting large pore sizes and ordered mesoporous structures were synthesized at low reaction (15°C) and high hydrothermal (160°C) temperatures via the co-condensation of tetraethoxysilane (TEOS) with a suite of organosilanes, i.e., 3-aminopropyltriethoxysilane (APTES), 3-mercaptopropyltrimethoxysilane (MPTMS), vinyltrimethoxysilane (VTMS), and phenyltrimethoxysilane (PTMS), in the presence of structure directing micelles formed using the surfactant pluronic F127 and the pore enlarging reagent trimethylbenzene (TMB). Small-angle X-ray scattering (SAXS) and transmission electron microscopy (TEM) confirmed that all synthesized materials possessed a face-centered cubic mesostructure (space group Fm3 j m), while nitrogen sorption analyses showed that the synthesized materials had extra large pores with cavity sizes of up to 25.4 nm and entrance sizes of up to 10.8 nm. X-ray photoelectron spectroscopy (XPS) and 13 C solid-state magic-angle spinning nuclear magnetic resonance ( 13 C-MAS NMR) measurements verified the incorporation of the different organosilanes into the silica network and more importantly on the inner and outer surfaces of the materials. As-obtained mesoporous silicas were tested in protein immobilization studies using bovine serum albumin and the cellulose-hydrolyzing enzyme cellulase, which in itself is a mixture of three large enzymes. Enzyme immobilization efficiency, activity, and stability varied significantly with organic functionality due to size exclusion effects at pore entries, electrostatic and hydrophobic interactions between the organo-functionalized surfaces and the enzymes, and conformational changes of the enzymes which can occur on some of the material surfaces. As a result, phenyl (PTMS)-and thiol (MPTMS)-functionalized FDU-12 mesoporous silicas had a very low adsorption capacity of proteins because of their small pore sizes. Amino (APTES)-functionalized FDU-12 mesoporous silica showed the highest adsorption amount of proteins yet the lowest activity of immobilized cellulase. Cellulase immobilization on vinyl (VTMS)-functionalized FDU-12 mesoporous silica appeared to be the most promising approach, since it occurred with high efficiency, maintained enzyme activity, and provided temporal enzyme stability.

show abstract

Section: Introductionmentioning

confidence: 99%

Functionalized Mesoporous Silica with Very Large Pores for Cellulase Immobilization

et al. 2010

Self Cite

View full text Add to dashboard Cite

show abstract

“…The encapsulation process was found to be very rapid, with over 95% encapsulation efficiency being achieved within twenty minutes for all proteins. 51,[71][72] It is also interesting to note that CAT (250 kDa, ca. 10 nm diameter) 52 can be encapsulated into the mesopore network despite the fact that the pore size is similar to that of protein.…”

Section: Protein Loading Studiesmentioning

confidence: 95%

Mesoporous Silica Nanoparticles with Large Pores for the Encapsulation and Release of Proteins

Tu¹,

Boyle²,

Friedrich

et al. 2016

ACS Appl. Mater. Interfaces

120

View full text Add to dashboard Cite

Mesoporous silica nanoparticles (MSNs) have been explored extensively as solid supports for proteins in biological and medical applications. Small (< 200 nm) MSNs with ordered large pores (> 5 nm), capable of encapsulating therapeutic small molecules suitable for delivery applications in vivo, are rare however. Here we present small, elongated, cuboidal, MSNs with average dimensions of 90 × 43 nm that possess disk-shaped cavities, stacked on top of each other, which run parallel to the short axis of the particle. Amine-functionalization was achieved by modifying the MSN surface with 3-aminopropyltriethoxysilane or 3-[2-(2-aminoethylamino)ethylamino] propyltrimethoxysilane (AP-MSNs and AEP-MSNs) and were shown to have similar dimensions to the non-functionalized MSNs. The dimensions of these particles, and their large surface areas as measured by nitrogen adsorption-desorption isotherms, make them ideal scaffolds for protein encapsulation and delivery. We therefore investigated the encapsulation and release behavior for seven model proteins (α-lactalbumin, ovalbumin, bovine serum albumin, catalase, hemoglobin, lysozyme and cytochrome c). It was discovered that all types of MSNs used in this study allow rapid encapsulation, with a high loading capacity, for all proteins studied. Furthermore, the release profiles of the proteins were tunable. The variation in both rate and amount of protein uptake and release was found to be determined by the surface chemistry of the MSNs, together with the isoelectric point (pI), and molecular weight of the proteins, as well as by the ionic strength of the buffer. These MSNs with their large surface area and optimal dimensions, provide a scaffold with a high encapsulation efficiency and controllable release profiles for a variety of proteins, enabling potential applications in fields such as drug delivery and protein therapy.

show abstract

“…31,52,55 LP-FDU-12-TMB-C and LP-FDU-12-XYL-C exhibited well-resolved patterns characteristic of a face-centered cubic structure (Fm3m). 41,43,50 The unit-cell parameter was 40 nm and 46 nm, respectively. In the case of amorphous mesoporous materials (MCF-TIPB-C and PSSP), the XRD patterns only showed a broad diffraction peak at low angle, pointing to the absence of periodical order in the pore structure (see SI, Figure S1).…”

Section: Characterization Of the Silica Supports Usedmentioning

confidence: 99%

Oriented Coimmobilization of Oxidase and Catalase on Tailor-Made Ordered Mesoporous Silica

et al. 2017

View full text Add to dashboard Cite

Mesoporous silica materials are promising carriers for enzyme immobilization in heterogeneous biocatalysis applications. By tailoring their pore structural framework, these materials are designable for appropriate enzyme binding capacity and internal diffusivity. To supply O 2 efficiently to solid-supported immobilized enzymes represents a core problem of heterogeneously catalyzed oxidative biotransformations. In this study, therefore, we synthesized and compared three internally well-ordered and two amorphous silica materials as enzyme carriers, each of those with pore sizes of ≥10 nm, to enable the co-immobilization of D-aminoacid oxidase (93 kDa) and catalase (245 kDa). Both enzymes were fused to the silica-binding module Z basic2 to facilitate their selective and oriented immobilization directly from crude protein mixtures on native silica materials. Analyzing the effects of varied pore architecture and internal surface area on the performance of the immobilized bienzymatic system, we showed that a uniform pore structural framework was beneficial for enzyme loading (≥ 70 mg protein/g carrier), immobilization yield (≥ 90%), surface and pore volume filling without hindered adsorption, and catalytic effectiveness (≥ 60%) of the co-immobilizate. Using the best carrier LP-SBA-15, we obtained a solid oxidase-catalase preparation with an activity of 2000 µmol/(min g_material) that was recyclable and stable during oxidation of D-methionine. These results affirm a strategy of optimizing immobilized O 2 -dependent enzymes via tunable internal structuring of the silica material used as carrier. They thus make a significant advance towards the molecular design of heterogeneous oxidation biocatalysts on mesoporous silica supports.

show abstract

Improving Adsorbent Properties of Cage-like Ordered Amine Functionalized Mesoporous Silica with Very Large Pores for Bioadsorption

Cited by 137 publications

References 56 publications

Functionalized Mesoporous Silica with Very Large Pores for Cellulase Immobilization

Functionalized Mesoporous Silica with Very Large Pores for Cellulase Immobilization

Mesoporous Silica Nanoparticles with Large Pores for the Encapsulation and Release of Proteins

Oriented Coimmobilization of Oxidase and Catalase on Tailor-Made Ordered Mesoporous Silica

Contact Info

Product

Resources

About