ArticleBMC biotechnology2015
Cold shock induction of recombinant Arctic environmental genes.
Article in BMC biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Engineering a Potent Anti-MRSA Agent: The Development and Characterization of Chimeric Endolysin ZAM-MSC.Iranian biomedical journal · 2025Article
- Delaying production with prokaryotic inducible expression systems.Microbial cell factories · 2024Review
- The potential of cold-shock promoters for the expression of recombinant proteins in microbes and mammalian cells.Journal, genetic engineering & biotechnology · 2022Review
- pCold-assisted expression of a thermostable xylanase from3 Biotech · 2022Article
- Cold Adaptation Strategies and the Potential of Psychrophilic Enzymes from the Antarctic Yeast,Journal of fungi (Basel, Switzerland) · 2021Review
- Enhanced Recombinant Protein Production Under Special Environmental Stress.Frontiers in microbiology · 2021Review
- Laboratory Evolution of GH11 Endoxylanase Through DNA Shuffling: Effects of Distal Residue Substitution on Catalytic Activity and Active Site Architecture.Frontiers in bioengineering and biotechnology · 2019Article
- Expression of soluble native protein inBiotechnology reports (Amsterdam, Netherlands) · 2018Article
- Development of Versatile Vectors for Heterologous Expression inMicroorganisms · 2018Article
- Engineering low-temperature expression systems for heterologous production of cold-adapted enzymes.Bioengineered · 2016Article
- Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.Frontiers in microbiology · 2016Review
- Biochemical Characterization of a Family 15 Carbohydrate Esterase from a Bacterial Marine Arctic Metagenome.PloS one · 2016Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundHeterologous expression of psychrophilic enzymes in E. coli is particularly challenging due to their intrinsic instability. The low stability is regarded as a consequence of adaptation that allow them to function at low temperatures. Recombinant production presents a significant barrier to their exploitation for commercial applications in industry.
methodsAs part of an enzyme discovery project we have investigated the utility of a cold-shock inducible promoter for low-temperature expression of five diverse genes derived from the metagenomes of marine Arctic sediments. After evaluation of their production, we further optimized for soluble production by building a vector suite from which the environmental genes could be expressed as fusions with solubility tags.
resultsWe found that the low-temperature optimized system produced high expression levels for all putatively cold-active proteins, as well as reducing host toxicity for several candidates. As a proof of concept, activity assays with one of the candidates, a putative chitinase, showed that functional protein was obtained using the low-temperature optimized vector suite.
conclusionsWe conclude that a cold-shock inducible system is advantageous for the heterologous expression of psychrophilic proteins, and may also be useful for expression of toxic mesophilic and thermophilic proteins where properties of the proteins are deleterious to the host cell growth.
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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.