ArticlePloS one2016
Exploring the Mechanism Responsible for Cellulase Thermostability by Structure-Guided Recombination.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 49 citations in OpenAlex.
- Corn Steep Liquor as an Efficient Bioresource for Functional Components Production by Biotransformation Technology.Foods (Basel, Switzerland) · 2025Review
- High-resolution protein modeling through Cryo-EM and AI: current trends and future perspectives - a review.Frontiers in molecular biosciences · 2025Review
- The S-S bridge mutation between the A2 and A4 loops (T416C-I432C) of Cel7A ofApplied and environmental microbiology · 2024Article
- Biochemical and structural characterisation of a family GH5 cellulase from endosymbiont of shipworm P. megotara.Biotechnology for biofuels and bioproducts · 2023Article
- A unique self-truncation of bacterial GH5 endoglucanases leads to enhanced activity and thermostability.BMC biology · 2022Article
- Cellulases: From Bioactivity to a Variety of Industrial Applications.Biomimetics (Basel, Switzerland) · 2021Review
- Molecular cloning and characterization of a thermostable and halotolerant endo-β-1,4-glucanase from3 Biotech · 2021Article
- Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective.Frontiers in bioengineering and biotechnology · 2021Review
- Article
- Engineering Robust Cellulases for Tailored Lignocellulosic Degradation Cocktails.International journal of molecular sciences · 2020Review
- Cellulolytic thermophilic microorganisms in white biotechnology: a review.Folia microbiologica · 2020Review
- Activity and Thermostability of GH5 Endoglucanase Chimeras from Mesophilic and Thermophilic Parents.Applied and environmental microbiology · 2019Article
- An Archaeal Chitinase With a Secondary Capacity for Catalyzing Cellulose and Its Biotechnological Applications in Shell and Straw Degradation.Frontiers in microbiology · 2019Article
Corrections and comments
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Authors and funding
12 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellulases from Bacillus and Geobacillus bacteria are potentially useful in the biofuel and animal feed industries. One of the unique characteristics of these enzymes is that they are usually quite thermostable. We previously identified a cellulase, GsCelA, from thermophilic Geobacillus sp. 70PC53, which is much more thermostable than its Bacillus homolog, BsCel5A. Thus, these two cellulases provide a pair of structures ideal for investigating the mechanism regarding how these cellulases can retain activity at high temperature. In the present study, we applied the SCHEMA non-contiguous recombination algorithm as a novel tool, which assigns protein sequences into blocks for domain swapping in a way that lessens structural disruption, to generate a set of chimeric proteins derived from the recombination of GsCelA and BsCel5A. Analyzing the activity and thermostability of this designed library set, which requires only a limited number of chimeras by SCHEMA calculations, revealed that one of the blocks may contribute to the higher thermostability of GsCelA. When tested against swollen Avicel, the highly thermostable chimeric cellulase C10 containing this block showed significantly higher activity (22%-43%) and higher thermostability compared to the parental enzymes. With further structural determinations and mutagenesis analyses, a 310 helix was identified as being responsible for the improved thermostability of this block. Furthermore, in the presence of ionic calcium and crown ether (CR), the chimeric C10 was found to retain 40% residual activity even after heat treatment at 90°C. Combining crystal structure determinations and structure-guided SCHEMA recombination, we have determined the mechanism responsible for the high thermostability of GsCelA, and generated a novel recombinant enzyme with significantly higher activity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.