ArticleBMC biotechnology2017
Conversion of an inactive xylose isomerase into a functional enzyme by co-expression of GroEL-GroES chaperonins in Saccharomyces cerevisiae.
Article in BMC biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 33 citations in OpenAlex.
- Multi-Omics Dissection and Functional Validation of Candidate Regulators Modulating Stress Tolerance and Xylose Utilization in the Natural Yeast Strain YB-2625.Journal of fungi (Basel, Switzerland) · 2026Article
- Systems-Level Metabolic Regulation Strategies of Xylose Metabolism in Saccharomyces cerevisiae.Biotechnology journal · 2026Review
- Systems metabolic engineering of glutathione biosynthesis inEngineering microbiology · 2025Article
- Engineering Saccharomyces Cerevisiae With Novel Functional Xylose Isomerases From Rumen Microbiota for Enhanced Biofuel Production.Biotechnology journal · 2025Article
- Compartmentalization of heme biosynthetic pathways into yeast mitochondria enhances heme production.NPJ science of food · 2025Article
- Systems Metabolic Engineering ofJournal of fungi (Basel, Switzerland) · 2024Article
- FromJournal of fungi (Basel, Switzerland) · 2023Review
- Engineering ofEngineering microbiology · 2023Review
- Big data mining, rational modification, and ancestral sequence reconstruction inferred multiple xylose isomerases for biorefinery.Science advances · 2023Article
- GroEL-A Versatile Chaperone for Engineering and a Plethora of Applications.Biomolecules · 2022Review
- Construction of advanced producers of first- and second-generation ethanol in Saccharomyces cerevisiae and selected species of non-conventional yeasts (Scheffersomyces stipitis, Ogataea polymorpha).Journal of industrial microbiology & biotechnology · 2020Review
- Molecular evolutionary engineering of xylose isomerase to improve its catalytic activity and performance of micro-aerobic glucose/xylose co-fermentation inBiotechnology for biofuels · 2019Article
- Optimizing anaerobic growth rate and fermentation kinetics inBiotechnology for biofuels · 2018Article
- Linking Microbial Community Structure and Function During the Acidified Anaerobic Digestion of Grass.Frontiers in microbiology · 2018Article
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSecond-generation ethanol production is a clean bioenergy source with potential to mitigate fossil fuel emissions. The engineering of Saccharomyces cerevisiae for xylose utilization is an essential step towards the production of this biofuel. Though xylose isomerase (XI) is the key enzyme for xylose conversion, almost half of the XI genes are not functional when expressed in S. cerevisiae. To date, protein misfolding is the most plausible hypothesis to explain this phenomenon.
resultsThis study demonstrated that XI from the bacterium Propionibacterium acidipropionici becomes functional in S. cerevisiae when co-expressed with GroEL-GroES chaperonin complex from Escherichia coli. The developed strain BTY34, harboring the chaperonin complex, is able to efficiently convert xylose to ethanol with a yield of 0.44 g ethanol/g xylose. Furthermore, the BTY34 strain presents a xylose consumption rate similar to those observed for strains carrying the widely used XI from the fungus Orpinomyces sp. In addition, the tetrameric XI structure from P. acidipropionici showed an elevated number of hydrophobic amino acid residues on the surface of protein when compared to XI commonly expressed in S. cerevisiae.
conclusionsBased on our results, we elaborate an extensive discussion concerning the uncertainties that surround heterologous expression of xylose isomerases in S. cerevisiae. Probably, a correct folding promoted by GroEL-GroES could solve some issues regarding a limited or absent XI activity in S. cerevisiae. The strains developed in this work have promising industrial characteristics, and the designed strategy could be an interesting approach to overcome the non-functionality of bacterial protein expression in yeasts.
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