Poly-(<scp>l</scp>)-histidine immobilized cryogels for lysozyme purification

Çimen, Duygu; Türkmen, Deniz; Deni̇zli̇, Adil

doi:10.1177/0263617416664453

Cited by 13 publications

(5 citation statements)

References 44 publications

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“…The average value of the maximum adsorptive capacity was approximately 360 mg/g for the three Tris‐cryogels in this work, which was comparable to or greater than the values reported in the literature [42,44,55‐59]. As shown in Table 2, the Tris ligand exhibited the highest affinity for lysozyme compared with the other ligands.…”

Section: Resultssupporting

confidence: 82%

“…Recently, lysozyme has been investigated for use as an anticancer drug and for the treatment of HIV infection [41]. Commercial lysozyme was purified from chicken egg white (CEW) using techniques including direct crystallization and precipitation, gel permeation chromatography and adsorption chromatography, membrane filtration, ion‐exchange chromatography, and affinity chromatography [42]. Among these techniques, affinity chromatography was relatively effective for protein purification because of the advantages of specific adsorption and a single‐step process.…”

Section: Introductionmentioning

confidence: 99%

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Preparation of supermacroporous cryogels with improved mechanical strength for efficient purification of lysozyme from chicken egg white

Sun

Feng

Zhong

et al. 2020

J of Separation Science

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A novel, facile, and robust strategy was proposed to increase the pore size and mechanical strength of cryogels. By mixing the monomers of acrylamide and 2‐hydroxyethyl methacrylate as the precursor, a monolithic copolymer cryogel with large interconnected pores and thick pore walls was prepared. Hydrogen bonding between the two monomers contributed to the entanglement and aggregation of the copolymers, thickening the pore walls and resulting in larger pore sizes. Analysis via mercury porosimetry demonstrated that the interconnected pore diameter of the copolymer cryogel ranged from 10‐350 µm, which was far larger than that of the cryogels from one monomer (10‐50 µm). Additionally, the thicker pore walls of the copolymer cryogel improved its mechanical strength. Affinity cryogels were prepared through covalent immobilization using Tris(hydroxymethyl)aminomethane as a coupling agent, and the affinity binding of lysozymes on Tris‐cryogel was evaluated by the Langmuir isothermal adsorption with the maximum adsorption capacity of 360 mg/g. Compared with that of the Tris‐cryogels produced from one monomer, the copolymer Tris‐cryogel exhibited higher adsorption capacity and lysozyme purity, when the chicken egg white solution flowed solely driven by gravity. This work provides a new avenue for designing and developing supermacroporous cryogels for bioseparation.

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Section: Resultssupporting

confidence: 82%

Section: Introductionmentioning

confidence: 99%

Preparation of supermacroporous cryogels with improved mechanical strength for efficient purification of lysozyme from chicken egg white

Sun

Feng

Zhong

et al. 2020

J of Separation Science

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“…The most important features that distinguish cryogels from other conventional matrices are their large porous structure, short diffusion path, and retention time. Recently, cryogels are accepted as the new generation fixed phase in separation technique [50]. Some studies on the purification of ovalbumin in the literature are summarized as follows.…”

Section: Discussionmentioning

confidence: 99%

Purification of Ovalbumin From Egg White Using Molecular Imprinted Cryogels

Çimen

Deni̇zli̇

2022

Hacettepe Journal of Biology and Chemistry

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S on yıllarda, dünya çapında gıda alerjisi en önemli sorunlardan biridir. Ovalbumin yumurta akında bulunan ana alerjanlardan biridir. Bu çalışmada, ovalbumin baskılanmış ve baskılanmamış poli(hidroksietil metakrilat-metakrilik asit) poli(HEMA-MAA) kriyojeller moleküler baskılama yöntemi kullanılarak sentezlenmiştir. Ovalbumin baskılanmış kriyojellerin karakterizasyonundan sonra, akış hızı, pH tamponu, ilk ovalbümin konsantrasyonu, iyonik kuvvet ve sıcaklık parametrelerinin etkisi incelenir. Maksimum ovalbumin adsorpsiyon miktarı, ovalbumin baskılanmış kriyojel için pH 5.5, 25°C ve 0.5 mL/dk akış hızında 37.78 mg/g olarak belirlenmiştir. Ovalbumin baskılanmış ve baskılanmamış kriyojellerin seçicilik çalışmaları, yarışmacı moleküller olarak lizozim ve transferrin kullanılarak gerçekleştirilmiştir. Ayrıca ovalbumin baskılanmış kriyojellerin yeniden kullanılabilirlik deneyleri gerçekleştirilmiştir. Ovalbuminin saflığı, sodyum-dodesil sülfat poliakrilamid jel elektroforezi (SDS-PAGE) kullanılarak yumurta akından belirlenmiştir. Ovalbuminin saflığı yaklaşık% 85.4 bulunmuştur.

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“…In this context, several polymeric compounds can be combined in the synthesis of cryogels, as well as the use of different freezing temperatures, as can be observed in Table 4. N-isopropilacrilamide + itaconic acid + N, N -methylene-bis-acrylamide Water APS + TEMED −22 [61] Acrylamide + N, N -methylene-bis-acrylamide + Alil-glycidyl ether Water APS + TEMED −12 [9,51] N-isopropilacrilamide + acrylic acid + N, N -methylene-bis-acrylamide Water APS + TEMED −22 [62] Poly-(L) -histidine + glycidil methacrylate (PGMA) + N -methylene-bis-acrylamide + HEMA Water APS + TEMED 16 [63] Acrylamide + lauryl acrylate + ethylene glycol dimethacrylate (EGDMA) Water PDMS + PBPO −18 [64] Poly (2-hydroxyethyl methacrylate) (PHEMA) Water APS + TEMED −12 [65] Here, APS: ammonium persulfate; TEMED: N, N, N, N tetramethylethylenediamine; HEMA: 2-hydroxyethyl methacrylate; Phenyl (2,4,6-trimethyl benzoyl)-phosphine oxide (PBPO); Poly (dimethyl siloxane) (PDMS). Source: adapted from [66].…”

Section: Monolithic Polymeric Cryogelsmentioning

confidence: 99%

Lectin Purification through Affinity Chromatography Exploiting Macroporous Monolithic Adsorbents

et al. 2023

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Growing medical, engineering, biochemical, and biological interest has led to a steady pace of research and development into polymeric monolithic structures with densely interconnected pores for purifying bio compounds. Cryogels, which are generated by freezing a reactive polymerization mixture, are highlighted due to their versatility and low relative cost as macroporous, polymeric, monolithic adsorbents. The conversion of cryogels into affinity adsorbents is one possible alternative to their optimal application. Some of the most often utilized supports for immobilizing particular ligands are monolithic columns manufactured with epoxy radicals on their surfaces. The purification of biomolecules with a high degree of specificity, such as lectins and glycoproteins with an affinity for glycosylated groups, has garnered interest in the use of fixed non-traditional beds functionalized with ligands of particular interest. The interaction is both robust enough to permit the adsorption of glycoproteins and reversible enough to permit the dissociation of molecules in response to changes in the solution’s pH. When compared to other protein A-based approaches, this one has been shown to be more advantageous than its counterparts in terms of specificity, ease of use, and cost-effectiveness. Information on polymeric, macroporous, monolithic adsorbents used in the affinity chromatographic purification of lectins has been published and explored.

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Poly-(l)-histidine immobilized cryogels for lysozyme purification

Cited by 13 publications

References 44 publications

Preparation of supermacroporous cryogels with improved mechanical strength for efficient purification of lysozyme from chicken egg white

Preparation of supermacroporous cryogels with improved mechanical strength for efficient purification of lysozyme from chicken egg white

Purification of Ovalbumin From Egg White Using Molecular Imprinted Cryogels

Lectin Purification through Affinity Chromatography Exploiting Macroporous Monolithic Adsorbents

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