Direct recovery of malate dehydrogenase from highly turbid yeast cell homogenate using dye-ligand affinity chromatography in stirred fluidized bed

Chen, Kuei-Hsiang; Lee, Sze Ying; Show, Pau Loke; Hong, Shih-Cheng; Chang, Yu-Kaung

doi:10.1016/j.jchromb.2018.09.039

Cited by 14 publications

(10 citation statements)

References 36 publications

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“…Good chemical stability [34,35] Low cost [34,35] High binding capacity [34,35] High reusability [34,35] Commercially available Ease of immobilization by covalent bonding on supports [36] Ease of large scale enzyme purification [37] Elution of the target protein is difficult [37] Synthetic affinity ligands, such as commercial triazine dyes have moderate selectivity [38] Care should be taken in the elution step in dye-ligand affinity chromatography [38] Cell affinity capture (CAC)…”

Section: Techniques Advantages Disadvantagesmentioning

confidence: 99%

“…Hence, HSA was effectively isolated using the developed sorbent [121]. In recent studies, different dye ligands have been employed on different supports like nanofiber membranes [34], chitosan matrix [122], streamline matrix [37], cellulose microfibers [123], cryogel membrane [124], silica [125], and various polymers [121,126,127] for separation of different biological molecules. A schematic representation of the interaction between cibacron blue F3G-A as a typical dye ligand and albumin is shown in Figure 6 [121].…”

Section: Dye-ligand Affinity Chromatographymentioning

confidence: 99%

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Recent trends in sorbents for bioaffinity chromatography

Kip

Hamaloğlu

Demir

et al. 2021

J of Separation Science

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Isolation or enrichment of biological molecules from complex biological samples is mostly a prerequisite in proteomics, genomics, and glycomics. Different techniques have been used to advance the efficiency of the purification of biological molecules. Bioaffinity chromatography is one of the most powerful technique that plays an important role in the isolation of target biological molecules by the specific interactions with ligands that are immobilized on different support materials. This review examines the recent developments in bioaffinity chromatography particularly over the past 5 years in the literature. Also properties of supports, immobilization techniques, types of binding agents, and methods used in bioaffinity chromatography applications are summarized.

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Section: Techniques Advantages Disadvantagesmentioning

confidence: 99%

Section: Dye-ligand Affinity Chromatographymentioning

confidence: 99%

Recent trends in sorbents for bioaffinity chromatography

Kip

Hamaloğlu

Demir

et al. 2021

J of Separation Science

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“…The triazine dye, CB3GA, is a well-established ligand in affinity chromatography [2,3,8,9,41]. The presence of hydrophobic, ionic and aromatic moieties in CB3GA give rise to the formation of mixed type interactions with proteins such as electrostatic, hydrophobic, hydrogen bonding interaction [11][12][13][20][21][22]43,44]. The presence of the chlorotriazine ring in CB3GA allows its direct immobilization onto the matrix.…”

Section: Synthesis Of the Affinity Adsorbentmentioning

confidence: 99%

“…Purification methods that are designed based on specific, effective and robust materials are expected to guide the future of the protein purification area [6,7]. Affinity chromatography is the most specialized method for the effective purification of proteins, compared to other separation methods [2][3][4][8][9][10][11][12][13]. It offers high selectivity, resolution, and capacity in most protein purification procedures.…”

Section: Introductionmentioning

confidence: 99%

“…In the present study, we employed the triazine dye Cibacron Blue 3GA (CB3GA) as an immobilized ligand. Triazine dyes display several advantages compared to specific biological ligands due to their low cost, resistance to biological and chemical degradation and high protein binding capacity [10][11][12][13][18][19][20][21][22]. In addition, the presence of the triazine ring allows their direct immobilization to the matrix (e.g., Sepharose or cellulose) through a nucleophilic substitution reaction [15,16].…”

Section: Introductionmentioning

confidence: 99%

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Reduce, Reuse and Recycle in Protein Chromatography: Development of an Affinity Adsorbent from Waste Paper and Its Application for the Purification of Proteases from Fish By-Products

Premetis

Labrou

2020

Biomolecules

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In the present study, we report the development of a cellulose-based affinity adsorbent and its application for the purification of proteases from fish by-products. The affinity adsorbent was synthesized using cellulose microfibers as the matrix, isolated from recycled newspapers using the acid precipitation method. As an affinity ligand, the triazine dye Cibacron Blue 3GA (CB3GA) was used and immobilized directly onto the cellulose microfibers. Absorption equilibrium studies and frontal affinity chromatography were employed to evaluate the chromatographic performance of the adsorbent using as model proteins bovine serum albumin (BSA) and lysozyme (LYS). Absorption equilibrium studies suggest that the adsorption of both proteins obeys the Langmuir isotherm model. The kinetics of adsorption obey the pseudo-second-order model. The affinity adsorbent was applied for the development of a purification procedure for proteases from Sparus aurata by-products (stomach and pancreas). A single-step purification protocol for trypsin and chymotrypsin was developed and optimized. The protocol afforded enzymes with high yields suitable for technical and industrial purposes.

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Affinity monolith chromatography: A review of general principles and recent developments

2021

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Affinity monolith chromatography (AMC) is a liquid chromatographic technique that utilizes a monolithic support with a biological ligand or related binding agent to isolate, enrich, or detect a target analyte in a complex matrix. The target‐specific interaction exhibited by the binding agents makes AMC attractive for the separation or detection of a wide range of compounds. This article will review the basic principles of AMC and recent developments in this field. The supports used in AMC will be discussed, including organic, inorganic, hybrid, carbohydrate, and cryogel monoliths. Schemes for attaching binding agents to these monoliths will be examined as well, such as covalent immobilization, biospecific adsorption, entrapment, molecular imprinting, and coordination methods. An overview will then be given of binding agents that have recently been used in AMC, along with their applications. These applications will include bioaffinity chromatography, immunoaffinity chromatography, immobilized metal‐ion affinity chromatography, and dye‐ligand or biomimetic affinity chromatography. The use of AMC in chiral separations and biointeraction studies will also be discussed.

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Direct recovery of malate dehydrogenase from highly turbid yeast cell homogenate using dye-ligand affinity chromatography in stirred fluidized bed

Cited by 14 publications

References 36 publications

Recent trends in sorbents for bioaffinity chromatography

Recent trends in sorbents for bioaffinity chromatography

Reduce, Reuse and Recycle in Protein Chromatography: Development of an Affinity Adsorbent from Waste Paper and Its Application for the Purification of Proteases from Fish By-Products

Affinity monolith chromatography: A review of general principles and recent developments

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