{
  "abstract": "High-temperature processing of carbohydrate-rich biomass, including starch liquefaction and lignocellulose saccharification, can improve sugar yields, reduce contamination risks, and facilitate integration with thermochemical pretreatments. However, the operational stability of native carbohydrate-active enzymes (CAZymes) at 60–90 °C remains a major bottleneck for efficient and economically viable biorefineries, and existing reviews rarely integrate multiscale molecular mechanisms with process-relevant engineering strategies. This review systematically examines the multiscale basis of thermostability in CAZymes—covering core hydrophobic packing, electrostatic and metal-mediated networks, disulfide bonds, conformational dynamics, and modular architectures involving catalytic domains, linkers, and carbohydrate-binding modules—and directly links these features to enzyme longevity under high-solids, inhibitor-rich conditions. We then critically compare key engineering strategies, including structure-guided rational design, semi-rational directed evolution, consensus design, ancestral sequence reconstruction, and machine learning-assisted workflows embedded in design–build–test–learn (DBTL) cycles, highlighting their respective strengths, limitations, and complementarity. Representative case studies demonstrate that engineered thermophilic α-amylases and cellulases achieving ΔTm improvements of approximately 10–20 °C can sustain >80–85% residual activity after prolonged exposure at process-relevant temperatures, translating into tangible benefits such as 15–30% reductions in enzyme dosing and measurable decreases in steam consumption, alongside higher sugar titers. By bridging molecular determinants, engineering paradigms, and quantitative process performance, this review provides a pragmatic roadmap for deploying thermostable CAZymes as robust biocatalysts in sustainable high-temperature biomass conversion.",
  "abstract_shown": true,
  "affiliations": [
    "College of Engineering and Applied Sciences, Nanjing University, Nanjing 210023, China",
    "School of Food and Pharmaceutical Engineering, Nanjing Normal University, Nanjing 210023, China"
  ],
  "article_type": "review article",
  "arxiv": null,
  "author_total": 8,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Yueli Hu"
    },
    {
      "affs": [
        1
      ],
      "name": "Xi Yang"
    },
    {
      "affs": [
        0
      ],
      "name": "Tianqi Wang"
    },
    {
      "affs": [
        1
      ],
      "name": "Mingshu Zheng"
    },
    {
      "affs": [
        0
      ],
      "name": "Zhenghao Jiang"
    },
    {
      "affs": [
        0
      ],
      "name": "Xinyue Dou",
      "orcid": "0009-0005-2700-6159"
    },
    {
      "affs": [
        0
      ],
      "name": "Xinkun Ren"
    },
    {
      "affs": [
        0
      ],
      "name": "Jiaxin Wu",
      "orcid": "0009-0006-0924-6922"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/695015k6f60mh.bib",
  "cited_by": 0,
  "doi": "10.3390/ijms27198788",
  "fulltext_url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13665343/?tool=EBI",
  "id": "695015k6f60mh",
  "issns": [
    "1422-0067"
  ],
  "landing_url": "https://europepmc.org/article/PMC/PMC13665343",
  "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|Enzyme Catalysis and Immobilization"
    ]
  ],
  "openalex": "W7214900368",
  "pdf_url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13665343/pdf/?tool=EBI",
  "pmcid": "PMC13665343",
  "pmid": null,
  "published": "2026-09-30",
  "publisher": "MDPI AG",
  "ris": "https://research.draconitic.com/paper/695015k6f60mh.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:35Z",
      "native_id": "PMC:PMC13665343",
      "source": "europepmc",
      "url": "https://europepmc.org/article/PMC/PMC13665343"
    },
    {
      "first_seen": "2026-10-30T12:18:55Z",
      "native_id": "10.3390/ijms27198788",
      "source": "crossref",
      "url": "https://www.mdpi.com/1422-0067/27/19/8788"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Enzyme Catalysis and Immobilization",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Thermostable Carbohydrate-Active Enzymes for High-Temperature Biomass Conversion: From Molecular Design to Process Integration",
  "title_text": "Thermostable Carbohydrate-Active Enzymes for High-Temperature Biomass Conversion: From Molecular Design to Process Integration",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:18:55Z",
  "url": "https://research.draconitic.com/paper/695015k6f60mh",
  "venue": "International journal of molecular sciences",
  "versions": []
}