{
  "abstract": "Controlling protein glycosylation as a critical quality attribute of biopharmaceuticals remains challenging when glycosylation is coupled to cellular production systems. Here, we present a proof-of-concept glycosyltransferase immobilised enzyme reactor (IMER) housed within a 3D-printed column that enables directed post-production glycan modification of purified glycoproteins. Using β-1,4-galactosyltransferase (B4GalT1-IMER) and α-2,6-sialyltransferase (ST6Gal1-IMER) immobilised on Ni-NTA resin, the IMER achieved near-complete galactosylation and substantial sialylation of partially de-glycosylated bovine fetuin N-glycans with their respective substrates with a maximum substrate-enzyme contact time of 4 minutes. Isomeric-level analysis revealed arm-specific addition preferences for both enzymes, consistent with known specificities. The modular IMER design permits sequential connection of individual enzyme chambers, potentially offering a scalable, plug-and-play platform for constructing defined glycan structures on recombinant glycoprotein therapeutics.",
  "abstract_shown": true,
  "affiliations": [
    "Institute for Biomedicine and Glycomics, Griffith University, Gold Coast, QLD, Australia.",
    "ARC Centre of Excellence in Synthetic Biology, Macquarie University, Sydney, NSW, Australia."
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 5,
  "authors": [
    {
      "affs": [
        0,
        1
      ],
      "name": "Nicholas J DeBono"
    },
    {
      "affs": [
        1
      ],
      "name": "Joel Cain"
    },
    {
      "affs": [
        0
      ],
      "name": "Chi-Hung Lin"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Nicolle H Packer",
      "orcid": "0000-0002-7532-4021"
    },
    {
      "affs": [
        1
      ],
      "name": "Edward S X Moh"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/2c9zzwq93cnpf.bib",
  "cited_by": 0,
  "doi": "10.3389/fmolb.2026.1932584",
  "fulltext_url": "https://europepmc.org/articles/PMC13690666",
  "id": "2c9zzwq93cnpf",
  "issns": [
    "2296-889X"
  ],
  "landing_url": "https://europepmc.org/article/MED/42920519",
  "language": "eng",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1312|Glycosylation and Glycoproteins Research"
    ]
  ],
  "openalex": "W7221192688",
  "pdf_url": "https://europepmc.org/articles/PMC13690666?pdf=render",
  "pmcid": "PMC13690666",
  "pmid": "42920519",
  "published": "2026-10-09",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/2c9zzwq93cnpf.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:20:33Z",
      "native_id": "MED:42920519",
      "source": "europepmc",
      "url": "https://europepmc.org/article/MED/42920519"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Glycosylation and Glycoproteins Research",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Immobilised enzyme reactors for post-production glycan modification of purified glycoproteins.",
  "title_text": "Immobilised enzyme reactors for post-production glycan modification of purified glycoproteins.",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:20:33Z",
  "url": "https://research.draconitic.com/paper/2c9zzwq93cnpf",
  "venue": "Frontiers in molecular biosciences",
  "versions": []
}