Applications of zeolite inorganic composites in biotechnology: Current state and perspectives

Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Noda-shi, Chiba-ken 278-8510, Japan.
Applied Microbiology and Biotechnology (Impact Factor: 3.34). 06/2005; 67(3):306-11. DOI: 10.1007/s00253-004-1782-4
Source: PubMed


The purpose of this short review is to introduce applications of inorganic composites, zeolites, in biotechnology. Although inorganic chemistry is generally considered distant from biotechnology, the two could be harmoniously integrated for biopolymer chromatography. New chromatographic carriers have been developed based on principles differing from those underlying conventional chromatography. Some can be used for the purification of proteins according to novel physicochemical principles, according to their isoelectric point (pI), molecular weight and shape. The amount of protein adsorbed is related to the pore size of the composites, which can recognize biomolecules with reference to these three parameters. Proteins adsorbed at their pI have been found to be desorbed at the pI by polyethylene glycol, but not by high ionic medium (NaCl), SDS, non-ionic detergents, ATP or urea. Therefore, inorganic composites synthesized in consideration of pore size and three-dimensional structure are suitable as new chromatographic carriers. Selective fractionation of biomaterials including proteins and nucleic acids should provide useful information regarding whether conjugated proteins in a precipitated state can be separated on net charge and whether cells can be directly fractionated in future.

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    • "Among different types of nanomaterials, zeolites have proven to be excellent alternatives for use in adsorption of biomolecules, like proteins, DNA, and RNA (Matsui et al. 2001; Sakaguchi et al. 2005; Chiku et al. 2003). One of the major advantages of incorporating zeolites into biosensor technologies is their tailorable surface groups, controlled hydrophilic/ hydrophobic properties, and the ability to alter the acidic/basic nature of zeolites by several methods (Rolison 1990). "
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    ABSTRACT: Analytical characteristics of urease- and butyrylcholinesterase (BuChE)- based ion sensitive field-effect transistor (ISFET) biosensors were investigated by the incorporation of zeolite Beta nanoparticles with varying Si/Al ratios. The results obtained by the zeolite-modified ISFET transducers suggested that the Si/Al ratio strongly influenced the biosensor performances due to the electrostatic interactions among enzyme, substrate, and zeolite surface as well as the nature of the enzymatic reaction. Using relatively small nanoparticles (62.7 ± 10, 76.2 ± 10, and 77.1 ± 10 nm) rather than larger particles, that are widely used in the literature, allow us to produce more homogenous products which will give more control over the quantity of materials used on the electrode surface and ability to change solely Si/Al ratio without changing other parameters such as particle size, pore volume, and surface area. This should enable the investigation of the individual effect of changing acidic and electronic nature of this material on the biosensor characteristics. According to our results, high biosensor sensitivity is evident on nanosize and submicron size particles, with the former resulting in higher performance. The sensitivity of biosensors modified by zeolite particles is higher than that to the protein for both types of biosensors. Most significantly, our results show that the performance of constructed ISFET-type biosensors strongly depends on Si/Al ratio of employed zeolite Beta nanoparticles as well as the type of enzymatic reaction employed. All fabricated biosensors demonstrated high signal reproducibility and stability for both BuChE and urease.
    Journal of Nanoparticle Research 05/2013; 15(5). DOI:10.1007/s11051-013-1645-y · 2.18 Impact Factor
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    • "Researchers have extensively reviewed that the immobilization of enzymes onto support matrices were through coupling mechanism for enhanced stability [12] [13] [14] [15] [16]. Many inorganic materials have been successfully used for the immobilization of enzymes [17] [18] [19] [20]. In our previous study, we detailed about the immobilization of lipase onto mesoporous activated carbon (MAC) (without chemical modification) [20]. "
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    ABSTRACT: This study deals with the surface functionalization of mesoporous activated carbon, using ethylenediamine and glutaraldehyde to facilitate the strong immobilization of acidic lipase (AL) onto MAC. The AL was produced from Pseudomonas gessardii by using slaughterhouse lipid waste as the substrate. The AL immobilized on functionalized mesoporous activated carbon (ALFMAC) was applied for the hydrolysis of waste cooked oil (WCO). The optimum conditions for the immobilization of AL onto functionalized mesoporous activated carbon (FMAC) were 90 min; pH 3.5; and 35 degrees C: which resulted at the maximum immobilization of 5440 U/g of FMAC (3.693 mg of AL/g of FMAC or the yield 2.7% or the expressed activity 103.7% or the activity per unit area of FMAC 1.08 mg of AL/m(2)). The ALFMAC showed better thermal and storage stabilities than the free AL The ALFMAC retained a 98% and a 92% initial activity at 40 degrees C and 50 degrees C. respectively, while the AL showed the thermal stability (residual activities) 65% and 38%, respectively. The storage stability of ALFMAC at 4 degrees C showed 100% initial activity up to 15 days from the initial day of the storage, whereas AL showed only 88% initial activity up to 15 days. The FMAC and ALFMAC were characterized by using scanning electron microscopy (SEM), Fourier transform infrared (FT-IR) spectroscopy, and X-ray diffraction (XRD) analysis. The K-m values of the ALFMAC and AL were 0.112 mM and 0.411 mM, respectively. The v(max) values of the ALFMAC and AL were 1.26 mM/min and 0.53 mM/min, respectively. Immobilization of AL onto FMAC obeyed the Freundlich and Redlich-Peterson isotherm models. The non-linear models of pseudo first, and second order, intra-particle diffusion, Bangham, and Boyd plot were also performed to understand the dynamic mechanism of immobilization. ALFMAC showed a 100% hydrolysis of WCO up to 21 cycles of reuse, and 60% up to 45 cycles. The hydrolysis of WCO was confirmed by using FT-IR spectra.
    PROCESS BIOCHEMISTRY 03/2012; 47(3):435-445. DOI:10.1016/j.procbio.2011.11.025 · 2.52 Impact Factor
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    • "Several natural polysaccharides, such as alginates, κ-carrageenan, agar, and agarose, are excellent gel materials and are widely used for entrapment [8]. Many other support materials for cell immobilization have been reported including delignified cellulosic material, chitosan [9]-[10], natural zeolite [11], g-alumina etc. Perspective techniques for yeasts immobilization can be divided into four categories: attachment or adsorption to solid surfaces (wood chips, delignified brewer's spent grains, DEAE cellulose, and porous glass), entrapment within a porous matrix (calcium alginate, k-carrageenan, polyvinyl alcohol, agar, gelatine, chitosan, and polyacrilamide), mechanical retention behind a barrier (microporous membrane filters, and microcapsules) and self-aggregation of the cells by flocculation. The application of these different immobilization methodologies and carriers, their impact in microbial growth and physiology, internal and external mass transfer limitations, product quality and consistency, bioreactor design, bioprocess engineering and economics have been largely discussed [12]-[13]-[14]-[15]-[16]. "
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    ABSTRACT: Saccharomyces cerevisiae cells were entrapped in matrix of alginate and magnetic nanoparticles and covalently immobilized on magnetite-containing chitosan and cellulose-coated magnetic nanoparticles. Cellulose-coated magnetic nanoparticles with covalently immobilized thermostable {\alpha}-amylase and chitosan particles with immobilized glucoamylase were also prepared. The immobilized cells and enzymes were applied in column reactors - 1/for simultaneous corn starch saccharification with the immobilized glucoamylase and production of ethanol with the entrapped or covalently immobilized yeast cells, 2/ for separate ethanol fermentation of the starch hydrolysates with the fixed yeasts. Hydrolysis of corn starch with the immobilized {\alpha}-amylase and glucoamylase, and separate hydrolysis with the immobilized {\alpha}-amylase were also examined. In the first reactor the ethanol yield reached approx. 91% of the theoretical; the yield was approx. 86% in the second. The ethanol fermentation was affected by the type of immobilization, the initial particle loading, feed sugar concentration and the dilution rate. The ethanol productivity with entrapped cells reached 264.0 g/L.h at particle loading rate 70% and dilution rate 3.0 h-1 with reducing sugar concentration of 200.0 g/L. The prepared magnetic particles with fixed yeast cells were stable at 4oC in saline for more than 1 month. .
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