Immobilization of lipase in cage-type mesoporous organosilicas via covalent bonding and crosslinking

Zhou, Zhou; Piepenbreier, Frank; Marthala, V. R. Reddy; Karbacher, Karl; Hartmann, Martin

doi:10.1016/j.cattod.2014.07.047

Cited by 54 publications

(39 citation statements)

References 58 publications

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“…With the use of three pairs of lipase‐immobilized zeolite Beta‐coated stainless steel porous discs (i.e., 12.84 U), a conversion of vinyl propionate of 65% was achieved within 8 h, while the yield of butyl propionate amounted to 45%. Although a comparison of the performance of the novel immobilization strategy with conventional catalysts prepared by immobilization (by physical adsorption, covalent anchoring, or cross‐linking) of lipase on silica or polymer supports is not straightforward, we observed that in particular the recycle stability is improved under similar experimental conditions while activity and selectivity of the catalysts are comparable …”

Section: Resultsmentioning

confidence: 88%

Zeolite‐Coated Porous Arrays: A Novel Strategy for Enzyme Encapsulation

Marthala

Friedrich

Zhou

et al. 2015

Adv Funct Materials

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Zeolite Beta-coated stainless steel supports with gradient porosity are employed as fi lter-panels for lipase encapsulation. Enzyme encapsulation on the stainless steel porous discs is achieved via vacuum infi ltration. Subsequently, two lipase-encapsulated zeolite Beta-coated stainless steel discs are attached using an adhesive. The zeolite Beta layer on the stainless steel discs largely prevents lipase leaching in comparison to the stainless steel discs without a zeolite layer. The activity of the lipase-encapsulated, attached zeolite Beta-coated stainless steel porous discs depends on the thickness of the zeolite Beta layer. It is shown that the biocatalytic performance of the lipaseencapsulated, attached zeolite Beta-coated stainless steel supports with a zeolite Beta layer thickness of ≈0.7-1 µm is better than the lipase-encapsulated, attached zeolite Beta-coated stainless steel supports with a zeolite Beta layer thickness of ≈2-3 µm in the lipase-catalyzed transesterifi cation of vinyl propionate with 1-butanol using n -hexane as solvent.

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Section: Resultsmentioning

confidence: 88%

Zeolite‐Coated Porous Arrays: A Novel Strategy for Enzyme Encapsulation

Marthala

Friedrich

Zhou

et al. 2015

Adv Funct Materials

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“…Therefore, MCM-41, a typical mesoporous silica, has been adopted to coat the Fe 3 O 4 nanoparticles and form a core-shell structure with high specific surface area, regular hexagonal ordered pores, adjustable pore size, ease of functionalization, etc. (Zhou et al, 2015;Yoon et al, 2003;Ye et al, 2006;Wang, 2006;Xu et al, 2014).…”

Section: Introductionmentioning

confidence: 98%

“…With the development of nanotechnology, many enzymes have been immobilized onto ferric silica nanoparticles, such as lipase, cholesterol oxidase, or haloalkane (Zhou et al, 2015;Šulek et al, 2010;Lin et al, 2014), in which lipase is the most common enzyme for immobilization. To date, lipase has been immobilized on various supports such as silica spheres (Yang et al, 2013), magnetic nanoparticles (Park et al, 2011), chitosan (Chiou & Wu, 2004) etc., in which magnetic nanoparticles are present as new supporting materials, especially for Fe 3 O 4 nanoparticles.…”

Section: Introductionmentioning

confidence: 99%

Characterization and optimization of mesoporous magnetic nanoparticles for immobilization and enhanced performance of porcine pancreatic lipase

et al. 2015

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In this paper, Fe3O4 nanoparticles coated with mesoporous silica were prepared successfully, noted as Fe3O4 at the mobile composition of matter No. 41 (MCM-41). Also, Fe3O4 at MCM-41 was grafted by both 3-aminopropyltriethoxysilane (APTS) and 3-chloropropyltriethoxysilane (CPS), noted as Fe3O4 at MCM-41/APTS and Fe3O4 at MCM-41/CPS. The compounds were characterized by X-ray powder diffraction, scanning electron microscopy, transmission electron microscopy, Fourier transform infrared spectroscopy, vibrating sample magnetometry, thermogravimetry and N2 adsorption/desorption. Then, the enzyme, porcine pancreas lipase (PPL), was immobilized onto these modified nanoparticles by covalent attachment, physical adsorption and cross-linking, noted as Fe3O4 at MCM-41/CPS-PPL, Fe3O4 at MCM-41-PPL and Fe3O4 at MCM-41/APTS-PPL, respectively. The results showed that Fe3O4 at MCM-41/CPS was the best nanomaterial for PPL immobilization, exhibiting enhanced immobilization efficiency (maximum 96 %), maximum relative activity (up to 96 %), high stability and reusability (83 % 56 days and 86.7 % ten cycles). Additionally, it offered some other advantages, such as easy recycling and reuse, complying with the trend of green chemistry. Therefore, Fe3O4 at MCM-41/CPS in combination with a relevant method can be proposed for commercial applications.

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“…Immobead (Immobead‐Epx) is useful for adsorbing or forming covalent and multipoint covalent linkages with enzymes, due to the high surface area that results from its mesoporous nature, and the possibility of modifying the epoxy groups on its surface . Immobead 150 has been employed for the immobilization of formate dehydrogenase, lipase, α‐amylase, laccase and pullulanase . Several compounds have been used for modification of epoxy groups in commercial supports aiming to evaluate different methods of immobilization.…”

Section: Introductionmentioning

confidence: 99%

“…1,14,15 Immobead 150 has been employed for the immobilization of formate dehydrogenase, lipase, a-amylase, laccase and pullulanase. [16][17][18][19][20][21][22][23][24] Several compounds have been used for modification of epoxy groups in commercial supports aiming to evaluate different methods of immobilization. Each compound provides its own characteristics to the material, such as the crosslinking of glutaraldehyde; oxidation through acid solution action to produce carboxyl groups; activation of carboxyl groups with 1,1-(3dimethylamino-propyl)-ethyl-carbodiimide hydrochloride by the reaction of nucleophilic agents on protonated carbodiimide, under slightly acid conditions, with amino groups of proteins, and addition of amine groups using ethylenediamine.…”

Section: Introductionmentioning

confidence: 99%

Modification of Immobead 150 support for protein immobilization: Effects on the properties of immobilized Aspergillus oryzae β‐galactosidase

Gennari

Mobayed

Rafael

et al. 2018

Biotechnology Progress

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We studied the modification of Immobead 150 support by either introducing aldehyde groups using glutaraldehyde (Immobead-Glu) or carboxyl groups through acid solution (Immobead-Ac) for enzyme immobilization by covalent attachment or ion exchange, respectively. These two types of immobilization were compared with the use of epoxy groups that are now provided on a commercial support. We used Aspergillus oryzae β-galactosidase (Gal) as a model protein, immobilizing it on unmodified (epoxy groups, Immobead-Epx) and modified supports. Immobilization yield and efficiency were tested as a function of protein loading (10-500 mg g support). Gal was efficiently immobilized on the Immobeads with an immobilization efficiency higher than 75% for almost all supports and protein loads. Immobilization yields significantly decreased when protein loadings were higher than 100 mg g support. Gal immobilized on Immobead-Glu and Immobead-Ac retained approximately 60% of its initial activity after 90 days of storage at 4°C. The three immobilized Gal derivatives presented higher half-lifes than the soluble enzyme, where the half-lifes were twice higher than the free Gal at 73°C. All the preparations were moderately operationally stable when tested in lactose solution, whey permeate, cheese whey, and skim milk, and retained approximately 50% of their initial activity after 20 cycles of hydrolyzing lactose solution. The modification of the support with glutaraldehyde provided the most stable derivative during cycling in cheese whey hydrolysis. Our results suggest that the Immobead 150 is a promising support for Gal immobilization. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 34:934-943, 2018.

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Immobilization of lipase in cage-type mesoporous organosilicas via covalent bonding and crosslinking

Cited by 54 publications

References 58 publications

Zeolite‐Coated Porous Arrays: A Novel Strategy for Enzyme Encapsulation

Zeolite‐Coated Porous Arrays: A Novel Strategy for Enzyme Encapsulation

Characterization and optimization of mesoporous magnetic nanoparticles for immobilization and enhanced performance of porcine pancreatic lipase

Modification of Immobead 150 support for protein immobilization: Effects on the properties of immobilized Aspergillus oryzae β‐galactosidase

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