Enhancing acetic acid and 5?hydroxymethyl furfural tolerance of C. saccharoperbutylacetonicum through adaptive laboratory evolution

نویسندگان

چکیده

In this study, adaptive laboratory evolution (ALE) was applied to isolate four strains of Clostridium saccharoperbutylacetonicum able grow in the presence hemicellulosic hydrolysate inhibitors unsupported by parental strain. Among them, RAC-25 presented best fermentative performance, producing 22.1 g/L ABE and 16.7 butanol. Genome sequencing revealed a deletion arabinose transcriptional repressor gene (araR) mutation anti-sigma factor I that promoted downregulation sigI. Gene expression analysis indicated high genes related H+-pumps (ATP synthases), proline biosynthesis (gamma phosphate reductase) chaperonins (Grol), suggesting an integrated mechanism is probably coordinated repression Therefore, addition highlighting power ALE for selecting robust strains, our results suggest sigI araR may be interesting targets increased tolerance toward inhibitor compounds relevant lignocellulosic biofuels production.

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

A new laboratory evolution approach to select for constitutive acetic acid tolerance in Saccharomyces cerevisiae and identification of causal mutations

BACKGROUND Acetic acid, released during hydrolysis of lignocellulosic feedstocks for second generation bioethanol production, inhibits yeast growth and alcoholic fermentation. Yeast biomass generated in a propagation step that precedes ethanol production should therefore express a high and constitutive level of acetic acid tolerance before introduction into lignocellulosic hydrolysates. However...

متن کامل

Improved thermostability and acetic acid tolerance of Escherichia coli via directed evolution of homoserine o-succinyltransferase.

In Escherichia coli, growth is limited at elevated temperatures mainly because of the instability of a single enzyme, homoserine o-succinyltransferase (MetA), the first enzyme in the methionine biosynthesis pathway. The metA gene from the thermophile Geobacillus kaustophilus cloned into the E. coli chromosome was found to enhance the growth of the host strain at elevated temperature (44 degrees...

متن کامل

Improvement of yeast tolerance to acetic acid through Haa1 transcription factor engineering: towards the underlying mechanisms

BACKGROUND Besides being a major regulator of the response to acetic acid in Saccharomyces cerevisiae, the transcription factor Haa1 is an important determinant of the tolerance to this acid. The engineering of Haa1 either by overexpression or mutagenesis has therefore been considered to be a promising avenue towards the construction of more robust strains with improved acetic acid tolerance. ...

متن کامل

Alcohols enhance the rate of acetic acid diffusion in S. cerevisiae: biophysical mechanisms and implications for acetic acid tolerance

Microbial cell factories with the ability to maintain high productivity in the presence of weak organic acids, such as acetic acid, are required in many industrial processes. For example, fermentation media derived from lignocellulosic biomass are rich in acetic acid and other weak acids. The rate of diffusional entry of acetic acid is one parameter determining the ability of microorganisms to ...

متن کامل

Thermal and solvent stress cross-tolerance conferred to Corynebacterium glutamicum by adaptive laboratory evolution.

Reinforcing microbial thermotolerance is a strategy to enable fermentation with flexible temperature settings and thereby to save cooling costs. Here, we report on adaptive laboratory evolution (ALE) of the amino acid-producing bacterium Corynebacterium glutamicum under thermal stress. After 65 days of serial passage of the transgenic strain GLY3, in which the glycolytic pathway is optimized fo...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Process Biochemistry

سال: 2021

ISSN: ['1359-5113', '1873-3298']

DOI: https://doi.org/10.1016/j.procbio.2020.11.013