ReviewMicrobial cell factories2017
Bottleneck in secretion of α-amylase in Bacillus subtilis.
Review in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed, 48 citations in OpenAlex.
- 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
- Isolation and characterization of the novel lytic Bacillus subtilis phage vB_Bsu_W1188 revealing a wall teichoic acid glycosylation-dependent resistance mechanism.Archives of virology · 2026Article
- Article
- Profiling of Metabolite Changes in Lettuce Leaves during Fermentation byJournal of microbiology and biotechnology · 2025Article
- Article
- Genome-Wide CRISPRi Screening of Key Genes for Recombinant Protein Expression in Bacillus Subtilis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- The Construction of an Environmentally Friendly Super-Secreting Strain ofInternational journal of molecular sciences · 2024Article
- Article
- Bacillus and Streptomyces spp. as hosts for production of industrially relevant enzymes.Applied microbiology and biotechnology · 2024Review
- Automation-aided construction and characterization ofFrontiers in bioengineering and biotechnology · 2024Article
- Microbial Secondary Metabolites via Fermentation Approaches for Dietary Supplementation Formulations.Molecules (Basel, Switzerland) · 2023Review
- Mining for novel cyclomaltodextrin glucanotransferases unravels the carbohydrate metabolism pathway via cyclodextrins in Thermoanaerobacterales.Scientific reports · 2022Article
- The impact of PrsA over-expression on theFrontiers in microbiology · 2022Article
- Effects of probiotics on loperamide-induced constipation in rats.Scientific reports · 2021Article
- Status of the application of exogenous enzyme technology for the development of natural plant resources.Bioprocess and biosystems engineering · 2021Review
- Shotgun sequence-based metataxonomic and predictive functional profiles of Pe poke, a naturally fermented soybean food of Myanmar.PloS one · 2021Article
- Bacillus subtilis: a universal cell factory for industry, agriculture, biomaterials and medicine.Microbial cell factories · 2020Review
- Establishment of a functional system for recombinant production of secreted proteins at 50 °C in the thermophilic Bacillus methanolicus.Microbial cell factories · 2020Article
- Genetically Modified Micro-Organisms for Industrial Food Enzyme Production: An Overview.Foods (Basel, Switzerland) · 2020Review
- Proteases HtrA and HtrB for α-amylase secreted from Bacillus subtilis in secretion stress.Cell stress & chaperones · 2019Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amylase plays an important role in biotechnology industries, and Gram-positive bacterium Bacillus subtilis is a major host to produce heterogeneous α-amylases. However, the secretion stress limits the high yield of α-amylase in B. subtilis although huge efforts have been made to address this secretion bottleneck. In this question-oriented review, every effort is made to answer the following questions, which look simple but are long-standing, through reviewing of literature: (1) Does α-amylase need a specific and dedicated chaperone? (2) What signal sequence does CsaA recognize? (3) Does CsaA require ATP for its operation? (4) Does an unfolded α-amylase is less soluble than a folded one? (5) Does α-amylase aggregate before transporting through Sec secretion system? (6) Is α-amylase sufficient stable to prevent itself from misfolding? (7) Does α-amylase need more disulfide bonds to be stabilized? (8) Which secretion system does PrsA pass through? (9) Is PrsA ATP-dependent? (10) Is PrsA reused after folding of α-amylase? (11) What is the fate of PrsA? (12) Is trigger factor (TF) ATP-dependent? The literature review suggests that not only the most of those questions are still open to answers but also it is necessary to calculate ATP budget in order to better understand how B. subtilis uses its energy for production and secretion.
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Registered trials
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.