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Molecular Decoration of Ceramic Supports for Highly Effective Enzyme Immobilization-Material Approach.

ABSTRACT: A highly effective method was developed to functionalize ceramic supports (Al₂O₃ powders and membranes) using newly synthesized spacer molecules. The functionalized materials were subsequently utilized for Candida antarctica lipase B enzyme immobilization. The objective is to systematically evaluate the impact of various spacer molecules grafted onto the alumina materials will affect both the immobilization of the enzymes and specific material surface properties, critical to enzymatic reactors performance. The enzyme loading was significantly improved for the supports modified with shorter spacer molecules, which possessed higher grafting effectiveness on the order of 90%. The specific enzyme activity was found to be much higher for samples functionalized with longer modifiers yielding excellent enantioselectivity >97%. However, the enantiomeric ratio of the immobilized lipase was slightly lower in the case of shorter spacer molecules.

SUBMITTER: Kujawa J

PROVIDER: S-EPMC7794798 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature

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Molecular Decoration of Ceramic Supports for Highly Effective Enzyme Immobilization-Material Approach.

Kujawa Joanna J Głodek Marta M Koter Izabela I Ośmiałowski Borys B Knozowska Katarzyna K Al-Gharabli Samer S Dumée Ludovic F LF Kujawski Wojciech W

Materials (Basel, Switzerland) 20210103 1

A highly effective method was developed to functionalize ceramic supports (Al2O3 powders and membranes) using newly synthesized spacer molecules. The functionalized materials were subsequently utilized for Candida antarctica lipase B enzyme immobilization. The objective is to systematically evaluate the impact of various spacer molecules grafted onto the alumina materials will affect both the immobilization of the enzymes and specific material surface properties, cri ...[more]

PMID: 33401646

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Project description:The high porosity, interconnected pore structure, and high surface area-to-volume ratio make the hydrophilic nonwoven nanofiber membranes (NV-NF-Ms) promising nanostructured supports for enzyme immobilization in different biotechnological applications. In this work, NV-NF-Ms with excellent mechanical and chemical properties were designed and fabricated by electrospinning in one step without using additives or complicated crosslinking processes after electrospinning. To do so, two types of ultrahigh-molecular-weight linear copolymers with very different mechanical properties were used. Methyl methacrylate-co-hydroxyethyl methacrylate (p(MMA)-co-p(HEMA)) and methyl acrylate-co-hydroxyethyl acrylate (p(MA)-co-p(HEA)) were designed and synthesized by reverse atom transfer radical polymerization (reverse-ATRP) and copper-mediated living radical polymerization (Cu0-MC-LRP), respectively. The copolymers were characterized by nuclear magnetic resonance (1H-NMR) spectroscopy and by triple detection gel permeation chromatography (GPC). The polarity, topology, and molecular weight of the copolymers were perfectly adjusted. The polymeric blend formed by (MMA)1002-co-(HEMA)1002 (M w = 230,855 ± 7418 Da; M n = 115,748 ± 35,567 Da; PDI = 2.00) and (MA)11709-co-(HEA)7806 (M w = 1.972 × 106 ± 33,729 Da; M n = 1.395 × 106 ± 35,019 Da; PDI = 1.41) was used to manufacture (without additives or chemical crosslinking processes) hydroxylated nonwoven nanofiber membranes (NV-NF-Ms-OH; 300 nm in fiber diameter) with excellent mechanical and chemical properties. The morphology of NV-NF-Ms-OH was studied by scanning electron microscopy (SEM). The suitability for enzyme binding was proven by designing a palette of different surface functionalization to enable both reversible and irreversible enzyme immobilization. NV-NF-Ms-OH were successfully functionalized with vinyl sulfone (281 ± 20 μmol/g), carboxyl (560 ± 50 μmol/g), and amine groups (281 ± 20 μmol/g) and applied for the immobilization of two enzymes of biotechnological interest. Galactose oxidase was immobilized on vinyl sulfone-activated materials and carboxyl-activated materials, while laccase was immobilized onto amine-activated materials. These preliminary results are a promising basis for the application of nonwoven membranes in enzyme technology.

Project description:In recent years, 3D printing has emerged in the field of chemical engineering as a powerful manufacturing technique to rapidly design and produce tailor-made reaction equipment. In fact, reactors with complex internal geometries can be easily fabricated, optimized and interchanged in order to respond to precise process needs, such as improved mixing and increased surface area. These advantages make them interesting especially for catalytic applications, since customized structured bed reactors can be easily produced. 3D printing applications are not limited to reactor design, it is also possible to realize functional low cost alternatives to analytical equipment that can be used to increase the level of process understanding while keeping the investment costs low. In this work, in-house designed ceramic structured inserts printed via vat photopolymerization (VPP) are presented and characterized. The flow behavior inside these inserts was determined with residence time distribution (RTD) experiments enabled by in-house designed and 3D printed inline photometric flow cells. As a proof of concept, these structured inserts were fitted in an HPLC column to serve as solid inorganic supports for the immobilization of the enzyme Phenolic acid Decarboxylase (bsPAD), which catalyzes the decarboxylation of cinnamic acids. The conversion of coumaric acid to vinylphenol was chosen as a model system to prove the implementation of these engineered inserts in a continuous biocatalytic application with high product yield and process stability. The setup was further automated in order to quickly identify the optimum operating conditions via a Design of Experiments (DoE) approach. The use of a systematic optimization, together with the adaptability of 3D printed equipment to the process requirements, render the presented approach highly promising for a more feasible implementation of biocatalysts in continuous industrial processes. Graphical abstract.Supplementary informationThe online version contains supplementary material available at 10.1007/s41981-021-00163-4.

Project description:A strategy for the bioconjugation of the enzyme Candida antarctica lipase B onto titania ceramic membranes with varied pore sizes (15, 50, 150, and 300 kDa) was successfully performed. The relationship between the membrane morphology, i.e.,the pore size of the ceramic support, and bioconjugation performance was considered. Owing to the dimension of the enzyme (~33 kDa), the morphology of the ceramics allowed (50, 150, and 300 kDa) or did not allow (15 kDa) the entrance of the enzyme molecules into the porous structure. Such a strategy made it possible to better understand the changes in the material (morphology) and physicochemical features (wettability, adhesiveness, and surface charge) of the samples, which were systematically examined. The silane functionalization and enzyme immobilization were accomplished via the covalent route. The samples were characterized after each stage of the modification, which was very informative from the material point of view. As a consequence of the modification, significant changes in the contact angle, roughness, adhesion, and zeta potential were observed. For instance, for the 50 kDa membrane, the contact angle increased from 29.1 ± 1.5° for the pristine sample to 72.3 ± 1.5° after silane attachment; subsequently, it was reduced to 57.2 ± 1.5° after the enzyme immobilization. Finally, the contact angle of the bioconjugated membrane used in the enzymatic process rose to 92.9 ± 1.5°. By roughness (Sq) controlling, the following amendments were noticed: for the pristine 50 kDa membrane, Sq = 1.87 ± 0.21 µm; after silanization, Sq = 2.33 ± 0.30 µm; after enzyme immobilization, Sq = 2.74 ± 0.26 µm; and eventually, after the enzymatic process, Sq = 2.37 ± 0.27 µm. The adhesion work of the 50 kDa samples was equal to 136.41 ± 2.20 mN m-1 (pristine membrane), 94.93 ± 2.00 mN m-1 (with silane), 112.24 ± 1.90 mN m-1 (with silane and enzyme), and finally, 69.12 ± 1.40 mN m-1 (after the enzymatic process). The materials and physicochemical features changed substantially, particularly after the application of the membrane in the enzymatic process. Moreover, the impact of ceramic material morphology on the zeta potential value is here presented for the first time. With an increase in the ceramic support cut-off, the amount of immobilized lipase rose, but the specific productivity was higher for membranes possessing smaller pores, owing to the higher grafting density. For the enzymatic process, two modes of accomplishment were selected, i.e., stirred-tank and cross-flow. The latter method was characterized by a much higher effectiveness, with a resulting productivity equal to 99.7 and 60.3 µmol h-1 for the 300 and 15 kD membranes, respectively.

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Molecular Decoration of Ceramic Supports for Highly Effective Enzyme Immobilization-Material Approach.

Publications

Molecular Decoration of Ceramic Supports for Highly Effective Enzyme Immobilization-Material Approach.

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