{
  "abstract": "Icariside I is a pharmacologically important prenylated flavonoid glycoside, yet its efficient biocatalytic production from icariin is hindered by the limited stability and recyclability of the enzymes involved. In this study, an α-L-rhamnosidase mutant R783A (Rha R783A) was heterologously expressed, purified, and immobilized within a Cu-based metal–organic framework (MOF) via a one-pot co-precipitation strategy. The resulting Rha R783A@MOF biocomposite exhibited enhanced stability compared to the free enzyme, retaining >90% residual activity after incubation at 60 °C for 2 h and 86.4% after 30 days of storage. It also demonstrated broad pH adaptability. In the biotransformation of icariin, Rha R783A@MOF achieved a 99.8% conversion rate and a 97.8% yield of icariside I. Furthermore, the biocomposite maintained an 88.9% yield after eight consecutive reuse cycles under high-temperature conditions (60 °C), demonstrating excellent operational stability. This work presents a robust and sustainable strategy for icariside I production, highlighting the potential of MOF microparticles as an effective platform for the biocatalytic synthesis of high-value flavonoid compounds.",
  "abstract_shown": true,
  "affiliations": [
    "School of Pharmacy, Henan University of Chinese Medicine, Zhengzhou 450046, China"
  ],
  "article_type": null,
  "arxiv": null,
  "author_total": 4,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Haoyu Jia"
    },
    {
      "affs": [
        0
      ],
      "name": "Tong Yan"
    },
    {
      "affs": [
        0
      ],
      "name": "Luran Wang"
    },
    {
      "affs": [
        0
      ],
      "name": "Lingling Song"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/3727vxhwqqgm8.bib",
  "cited_by": 0,
  "doi": "10.3390/molecules31203615",
  "fulltext_url": null,
  "id": "3727vxhwqqgm8",
  "issns": [
    "1420-3049"
  ],
  "landing_url": "https://www.mdpi.com/1420-3049/31/20/3615",
  "language": null,
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1312|Enzyme Catalysis and Immobilization"
    ]
  ],
  "openalex": "W7221551906",
  "pdf_url": null,
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-10",
  "publisher": "MDPI AG",
  "ris": "https://research.draconitic.com/paper/3727vxhwqqgm8.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:18:42Z",
      "native_id": "10.3390/molecules31203615",
      "source": "crossref",
      "url": "https://www.mdpi.com/1420-3049/31/20/3615"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Enzyme Catalysis and Immobilization",
      "subfield": "molecular-biology"
    }
  ],
  "title": "One-Pot Encapsulation of a Robust α-L-Rhamnosidase Mutant in Cu-MOF: A Recyclable Designed Biocatalyst for High-Yield Conversion of Icariin to Icariside I",
  "title_text": "One-Pot Encapsulation of a Robust α-L-Rhamnosidase Mutant in Cu-MOF: A Recyclable Designed Biocatalyst for High-Yield Conversion of Icariin to Icariside I",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:18:42Z",
  "url": "https://research.draconitic.com/paper/3727vxhwqqgm8",
  "venue": "Molecules",
  "versions": []
}