Search our Database of Scientific Publications and Authors

I’m looking for a

    Details and Download Full Text PDF:
    Conversion of an inactive xylose isomerase into a functional enzyme by co-expression of GroEL-GroES chaperonins in Saccharomyces cerevisiae.

    BMC Biotechnol 2017 Sep 9;17(1):71. Epub 2017 Sep 9.
    Laboratory of Genomics and Expression, Department of Genetics and Evolution, Institute of Biology, UNICAMP, Campinas, São Paulo, 13083-970, Brazil.
    Background: Second-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.

    Results: This 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.

    Conclusions: Based 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.
    PDF Download - Full Text Link
    ( Please be advised that this article is hosted on an external website not affiliated with PubFacts.com)
    Source Status
    http://dx.doi.org/10.1186/s12896-017-0389-7DOI ListingPossible
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5591498PMCFound

    Similar Publications

    Functional expression of xylose isomerase in flocculating industrial Saccharomyces cerevisiae strain for bioethanol production.
    J Biosci Bioeng 2016 Jun 30;121(6):685-691. Epub 2015 Nov 30.
    College of Architecture and Environment, Sichuan University, No. 24, South Section 1, First Ring Road, Chengdu 610065, China.
    Saccharomyces cerevisiae strains with xylose isomerase (XI) pathway were constructed using a flocculating industrial strain (YC-8) as the host. Both strains expressing wild-type xylA (coding XI) from the fungus Orpinomyces sp. and the bacterium Prevotella ruminicola, respectively, showed better growth ability and fermentation capacity when using xylose as the sole sugar than most of the reported strains expressing XI. Read More
    Bacterial xylose isomerases from the mammal gut Bacteroidetes cluster function in Saccharomyces cerevisiae for effective xylose fermentation.
    Microb Cell Fact 2015 May 17;14:70. Epub 2015 May 17.
    School of Life Sciences and Chemical Technology, Ngee Ann Polytechnic, Singapore, Singapore.
    Background: Xylose isomerase (XI) catalyzes the conversion of xylose to xylulose, which is the key step for anaerobic ethanolic fermentation of xylose. Very few bacterial XIs can function actively in Saccharomyces cerevisiae. Here, we illustrate a group of XIs that would function for xylose fermentation in S. Read More
    Development of efficient xylose fermentation in Saccharomyces cerevisiae: xylose isomerase as a key component.
    Adv Biochem Eng Biotechnol 2007 ;108:179-204
    Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC, Delft, The Netherlands.
    Metabolic engineering of Saccharomyces cerevisiae for ethanol production from D-xylose, an abundant sugar in plant biomass hydrolysates, has been pursued vigorously for the past 15 years. Whereas wild-type S. cerevisiae cannot ferment D-xylose, the keto-isomer D-xylulose can be metabolised slowly. Read More
    GroE chaperonins assisted functional expression of bacterial enzymes in Saccharomyces cerevisiae.
    Biotechnol Bioeng 2016 10 6;113(10):2149-55. Epub 2016 Apr 6.
    Carl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois.
    Rapid advances in the capabilities of reading and writing DNA along with increasing understanding of microbial metabolism at the systems-level have paved an incredible path for metabolic engineering. Despite these advances, post-translational tools facilitating functional expression of heterologous enzymes in model hosts have not been developed well. Some bacterial enzymes, such as Escherichia coli xylose isomerase (XI) and arabinose isomerase (AI) which are essential for utilizing cellulosic sugars, cannot be functionally expressed in Saccharomyces cerevisiae. Read More