ReviewInternational journal of molecular sciences2026
Thermostable Carbohydrate-Active Enzymes for High-Temperature Biomass Conversion: From Molecular Design to Process Integration.
Review in International journal of molecular sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Authors and funding
8 authors.
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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 ΔT
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