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Using EGFP as a model protein, commercially available bare iron oxide (BIONs) or silicon dioxide (BSiNs) nanoparticles as low\u2010cost purification\/immobilization matrices, and non\u2010hazardous and mild binding and elution conditions, adsorption and desorption studies were performed with lysates from <jats:italic>Escherichia coli\u2010<\/jats:italic>producing cells to compare the performance of these dual\u2010affinity tags. Under the conditions tested, the His6 tag stood out as the best\u2010performing tag, followed by CotB1p. Our findings concluded the promising combination of these tags, BIONs and BSiNs for one\u2010step purification of recombinant proteins, and two\u2010step purification and immobilization of recombinant proteins without intermediate buffer exchange. This proof of concept work set the ground for future evaluation of these purification and immobilization strategies using other proteins with different properties, which will be of interest to expand their utility and applicability.<\/jats:p>","DOI":"10.1002\/biot.202300152","type":"journal-article","created":{"date-parts":[[2023,7,21]],"date-time":"2023-07-21T15:14:25Z","timestamp":1689952465000},"source":"Crossref","is-referenced-by-count":12,"title":["Recombinant protein purification and immobilization strategies based on peptides with dual affinity to iron oxide and silica"],"prefix":"10.1002","volume":"18","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4368-7597","authenticated-orcid":false,"given":"Tatiana Q.","family":"Aguiar","sequence":"first","affiliation":[{"name":"CEB \u2013 Centre of Biological Engineering University of Minho  4710\u2010057 Braga Portugal"},{"name":"LABBELS \u2013 Associate Laboratory  Braga\/Guimar\u00e3es 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