ArticlePloS one2013
Fusing a carbohydrate-binding module into the Aspergillus usamii β-mannanase to improve its thermostability and cellulose-binding capacity by in silico design.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 42 citations in OpenAlex.
- Structural Characterization and Engineering of a GH134 β-Mannanase from Aspergillus nidulans for Enhancement of Activity and Stability.Journal of agricultural and food chemistry · 2026Article
- Engineering fusion enzymes for enhanced catalysis and stability: strategies and biotechnological applications.Molecular biology reports · 2026Review
- Enhancing the Catalytic Performance of β-Mannanase via Polyvinyl Alcohol Immobilization and Genipin Modification.Molecules (Basel, Switzerland) · 2025Article
- Structural and functional insights into cellulosomes: masters of plant cell wall degradation.Frontiers in microbiology · 2025Review
- Research and application progress of microbial β-mannanases: a mini-review.World journal of microbiology & biotechnology · 2024Review
- Recent advances in microbial and enzymatic engineering for the biodegradation of micro- and nanoplastics.RSC advances · 2024Review
- Multidomain chimeric enzymes as a promising alternative for biocatalysts improvement: a minireview.Molecular biology reports · 2024Review
- Article
- Impact of Starch Binding Domain Fusion on Activities and Starch Product Structure of 4-α-Glucanotransferase.Molecules (Basel, Switzerland) · 2023Article
- Engineering a carbohydrate-binding module to increase the expression level of glucoamylase in Pichia pastoris.Microbial cell factories · 2022Article
- Controlled Aggregation and Increased Stability of β-Glucuronidase by Cellulose Binding Domain Fusion.PloS one · 2017Article
- Cellulases and beyond: the first 70 years of the enzyme producer Trichoderma reesei.Microbial cell factories · 2016Review
- A chimeric α-amylase engineered from Bacillus acidicola and Geobacillus thermoleovorans with improved thermostability and catalytic efficiency.Journal of industrial microbiology & biotechnology · 2016Article
- Subsite-specific contributions of different aromatic residues in the active site architecture of glycoside hydrolase family 12.Scientific reports · 2015Article
- Catalytic efficiency of chitinase-D on insoluble chitinous substrates was improved by fusing auxiliary domains.PloS one · 2015Article
- A new acidophilic thermostable endo-1,4-β-mannanase from Penicillium oxalicum GZ-2: cloning, characterization and functional expression in Pichia pastoris.BMC biotechnology · 2014Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The AuMan5A, an acidophilic glycoside hydrolase (GH) family 5 β-mannanase derived from Aspergillus usamii YL-01-78, consists of an only catalytic domain (CD). To perfect enzymatic properties of the AuMan5A, a family 1 carbohydrate-binding module (CBM) of the Trichoderma reesei cellobiohydrolase I (TrCBH I), having the lowest binding free energy with cellobiose, was selected by in silico design, and fused into its C-terminus forming a fusion β-mannanase, designated as AuMan5A-CBM. Then, its encoding gene, Auman5A-cbm, was constructed as it was designed theoretically, and expressed in Pichia pastoris GS115. SDS-PAGE analysis displayed that both recombinant AuMan5A-CBM (reAuMan5A-CBM) and AuMan5A (reAuMan5A) were secreted into the cultured media with apparent molecular masses of 57.3 and 49.8 kDa, respectively. The temperature optimum of the reAuMan5A-CBM was 75°C, being 5°C higher than that of the reAuMan5A. They were stable at temperatures of 68 and 60°C, respectively. Compared with reAuMan5A, the reAuMan5A-CBM showed an obvious decrease in K m and a slight alteration in V max. In addition, the fusion of a CBM of the TrCBH I into the AuMan5A contributed to its cellulose-binding capacity.
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