ArticleBiomolecules2020
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.
Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 10 citations in OpenAlex.
- Preparation of Polymyxin B-Functionalized Cryogels for Efficient Endotoxin Removal from Protein Solutions.Gels (Basel, Switzerland) · 2025Article
- Prediction of the binding interactions between rosmarinic acid and cysteinyl leukotriene receptor type 1 by molecular docking and immobilized receptor chromatography.RSC advances · 2024Article
- Application of Biotechnological Techniques Aimed to Obtain Bioactive Compounds from Food Industry By-Products.Biomolecules · 2021Article
- Recent Advances in Supramolecular Affinity Separations: Affinity Chromatography and Related Methods.Advances in chromatography · 2021Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
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
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