Evidence map›Paper›PMID 42715962›Full record

ArticleJournal of agricultural and food chemistry2026

Structural Characterization and Engineering of a GH134 β-Mannanase from Aspergillus nidulans for Enhancement of Activity and Stability.

Sheng-Chia Chen, Po-Chih Kuo, Wen-Ming Chen, Shih-Yi Sheu, Yu-Bin Huang, Cheng-Yang Huang, I-Weh Chien, Tzong-Huei Lee, Chun-Hua Hsu

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Article in Journal of agricultural and food chemistry, 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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4 · The record

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5 · Who and what money

Authors and funding

9 authors.

Sheng-Chia ChenDepartment of Agricultural Chemistry, National Taiwan University, Taipei106319, Taiwan.
Po-Chih KuoDepartment of Agricultural Chemistry, National Taiwan University, Taipei106319, Taiwan.
Wen-Ming ChenDepartment of Seafood Science, National Kaohsiung University of Science and Technology, Kaohsiung811213, Taiwan.
Shih-Yi SheuDepartment of Marine Biotechnology, National Kaohsiung University of Science and Technology, Kaohsiung811213, Taiwan.
Yu-Bin HuangDepartment of Seafood Science, National Kaohsiung University of Science and Technology, Kaohsiung811213, Taiwan.
Cheng-Yang HuangDepartment of Agricultural Chemistry, National Taiwan University, Taipei106319, Taiwan.
I-Weh ChienDepartment of Agricultural Chemistry, National Taiwan University, Taipei106319, Taiwan.
Tzong-Huei LeeInstitute of Fisheries Sciences, National Taiwan University, Taipei106319, Taiwan.ORCID 0000-0001-8036-7563
Chun-Hua HsuDepartment of Agricultural Chemistry, National Taiwan University, Taipei106319, Taiwan.ORCID 0000-0002-0008-7383

Funding

National Science and Technology Council 111-2113-M-002-015-MY3National Science and Technology Council 111-2311-B-002-008-MY3National Science and Technology Council 114-2113-M-002-009-MY3National Taiwan University NTU-CC-113L894802National Taiwan University NTU-CC-114L893002National Taiwan University NTU-CC-115L891702
6 · The paper itself

Abstract

Mannans are abundant plant hemicelluloses, and endo-β-mannanases are important biocatalysts for their conversion into functional manno-oligosaccharides. Here, we report the structural and functional characterization of a glycoside hydrolase family 134 β-mannanase from Aspergillus nidulans (AnGH134) and a structure-guided engineering strategy to improve its performance on locust bean gum. The 1.75 Å crystal structure reveals the conserved lysozyme-like fold of GH134 enzymes and supports an inverting catalytic mechanism with Glu43 and Asp55 as the putative catalytic residues. Docking, mutational, and molecular dynamics analyses indicate that AnGH134 uses an extended substrate-binding groove and that groove-exit residues and the C-terminal region contribute to productive catalysis. Guided by these findings, N-terminal fusion of CBM10 enhanced catalytic efficiency and thermal stability, whereas C-terminal fusion was detrimental. These results provide a framework for engineering GH134 mannanases.

Indexed as

Aspergillus nidulansbeta-MannosidaseFungal ProteinsBiocatalysisEnzyme StabilityKineticsMannansProtein ConformationProtein EngineeringSubstrate Specificitybeta-MannosidaseFungal ProteinsMannansCBMcrystallographyGH134mannanaseprotein engineering

Identifiers

PMID42715962
PMCPMC13573560

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