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

Autor:	Nikolaos E. Labrou, Georgios Premetis
Rok vydání:	2020
Předmět:	Surface Properties lcsh:QR1-502 02 engineering and technology 01 natural sciences Biochemistry lcsh:Microbiology Chromatography Affinity Article Matrix (chemical analysis) chemistry.chemical_compound symbols.namesake affinity chromatography Adsorption Affinity chromatography medicine Animals Cellulose Bovine serum albumin Particle Size Molecular Biology Pancreas Triazine Waste Products fish by-products Chromatography biology Molecular Structure 010401 analytical chemistry Stomach Langmuir adsorption model Cibacron Blue 3GA 021001 nanoscience & nanotechnology Trypsin cellulose adsorbents Sea Bream 0104 chemical sciences chemistry biology.protein symbols proteases 0210 nano-technology medicine.drug Peptide Hydrolases
Zdroj:	Biomolecules Biomolecules, Vol 10, Iss 822, p 822 (2020) Volume 10 Issue 6
ISSN:	2218-273X
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5dceba671921e5050c221a211892488 https://pubmed.ncbi.nlm.nih.gov/32471269 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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