Publisher: American Chemical Society (ACS)

Issue: 18

License: [{"start"=>{"date-parts"=>[[2023, 4, 24]], "date-time"=>"2023-04-24T00:00:00Z", "timestamp"=>1682294400000}, "content-version"=>"vor", "delay-in-days"=>0, "URL"=>"https://creativecommons.org/licenses/by/4.0/"}]

Publication date(s): 2023/05/08 (print) 2023/04/24 (online)

Pages: 6829-6837

Volume: 11 Issue: 18

Journal: ACS Sustainable Chemistry & Engineering

Link: [{"URL"=>"https://pubs.acs.org/doi/pdf/10.1021/acssuschemeng.3c00517", "content-type"=>"application/pdf", "content-version"=>"vor", "intended-application"=>"unspecified"}, {"URL"=>"https://pubs.acs.org/doi/pdf/10.1021/acssuschemeng.3c00517", "content-type"=>"unspecified", "content-version"=>"vor", "intended-application"=>"similarity-checking"}]

URL: http://dx.doi.org/10.1021/acssuschemeng.3c00517

Reported herein is an entrapment method for enzyme immobilization that does not require the formation of new covalent bonds. Ionic liquid supramolecular gels are formed containing enzymes that can be shaped into gel beads and act as recyclable immobilized biocatalysts. The gel was formed from two components, a hydrophobic phosphonium ionic liquid and a low molecular weight gelator derived from the amino acid phenylalanine. Gel-entrapped lipase from Aneurinibacillus thermoaerophilus was recycled for 10 runs over 3 days without loss of activity and retained activity for at least 150 days. The procedure does not form covalent bonds upon gel formation, which is supramolecular, and no bonds are formed between the enzyme and the solid support.