ReviewBioengineered
How to achieve high-level expression of microbial enzymes: strategies and perspectives.
Review in Bioengineered. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 164 citations in OpenAlex.
- The acetylation mechanism and engineering strategy of isocitrate lyase for optimizing biosynthesis inSynthetic and systems biotechnology · 2026Article
- Overcoming cellular secretion bottlenecks: advanced secretion engineering and molecular tailoring for next-generation microbial α-amylases with enhanced industrial performance.World journal of microbiology & biotechnology · 2026Review
- Insect Gut Microbiota as a Reservoir of Industrially Relevant Enzymes: A Comprehensive Review.Microbial ecology · 2026Review
- Enhanced fibrinolytic enzyme production by Oidiodendron maius through green bioprocessing of agro-industrial residue.PloS one · 2026Article
- Oral Live-Carrier Vaccine of Recombinant Lactococcus lactis Inducing Prophylactic Protective Immunity Against Helicobacter pylori Infection.Probiotics and antimicrobial proteins · 2025Article
- A method for site-specifically tethering the enzyme urease to DNA origami with sustained activity.PloS one · 2025Article
- Cloning, heterologous expression and characterization of β-glucosidase deriving from3 Biotech · 2024Article
- Molecular Cloning, Characterization, and Application of Organic Solvent-Stable and Detergent-Compatible Thermostable Alkaline Protease fromJournal of microbiology and biotechnology · 2024Article
- DNA methylases for site-selective inhibition of type IIS restriction enzyme activity.Applied microbiology and biotechnology · 2024Article
- Recent Advances of Enzymes in the Food Industry.Foods (Basel, Switzerland) · 2023Article
- The oxygen-tolerant reductive glycine pathway assimilates methanol, formate and CONature communications · 2023Article
- Optimization, partial purification, and characterization of a novel high molecular weight alkaline protease produced by Halobacillus sp. HAL1 using fish wastes as a substrate.Journal, genetic engineering & biotechnology · 2023Article
- Standard Intein Gene Expression Ramps (SIGER) for Protein-Independent Expression Control.ACS synthetic biology · 2023Article
- An environment-benign approach of bamboo pulp bleaching using extracellular xylanase of strain Bacillus stratosphericus EB-11 isolated from elephant dung.Folia microbiologica · 2023Article
- Isolation and characterization of a novel hydrolase-producing probioticFrontiers in nutrition · 2023Article
- Controlling Specific Growth Rate for Recombinant Protein Production by Pichia pastoris Under Oxidation Stress in Fed-batch Fermentation.Applied biochemistry and biotechnology · 2022Article
- Efficient extracellular production of recombinant proteins in E. coli via enhancing expression of dacA on the genome.Journal of industrial microbiology & biotechnology · 2022Article
- Characterization of a novel thermophilic metagenomic GH5 endoglucanase heterologously expressed in Escherichia coli and Saccharomyces cerevisiae.Biotechnology for biofuels and bioproducts · 2022Article
- An improved whole-cell biotransformation system for (Food science & nutrition · 2022Article
- Mechano-chemical and biological energetics of immobilized enzymes onto functionalized polymers and their applications.Bioengineered · 2022Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microbial enzymes have been used in a large number of fields, such as chemical, agricultural and biopharmaceutical industries. The enzyme production rate and yield are the main factors to consider when choosing the appropriate expression system for the production of recombinant proteins. Recombinant enzymes have been expressed in bacteria (e.g., Escherichia coli, Bacillus and lactic acid bacteria), filamentous fungi (e.g., Aspergillus) and yeasts (e.g., Pichia pastoris). The favorable and very advantageous characteristics of these species have resulted in an increasing number of biotechnological applications. Bacterial hosts (e.g., E. coli) can be used to quickly and easily overexpress recombinant enzymes; however, bacterial systems cannot express very large proteins and proteins that require post-translational modifications. The main bacterial expression hosts, with the exception of lactic acid bacteria and filamentous fungi, can produce several toxins which are not compatible with the expression of recombinant enzymes in food and drugs. However, due to the multiplicity of the physiological impacts arising from high-level expression of genes encoding the enzymes and expression hosts, the goal of overproduction can hardly be achieved, and therefore, the yield of recombinant enzymes is limited. In this review, the recent strategies used for the high-level expression of microbial enzymes in the hosts mentioned above are summarized and the prospects are also discussed. We hope this review will contribute to the development of the enzyme-related research field.
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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.