ReviewInternational journal of molecular sciences2023
Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst.
Review in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Enzymatic Properties and Multifunctional Applications of a Novel Extracellular Cold-Active Alkaline Protease from Stenotrophomonas maltophilia Strain TK-4.Applied biochemistry and biotechnology · 2026Article
- Enzymatic valorization of fishery by-products: harnessing cold-adapted marine proteases for sustainable production of bioactive peptides.Archives of microbiology · 2025Review
- Enzymatic valorization of fishery by-products: harnessing cold-adapted marine proteases for sustainable production of bioactive peptides.Archives of microbiology · 2025Review
- Biochemical features and biotechnological potential of a proteolytic extract from a psychrophilic Antarctic bacterium.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2025Article
- Research Progress Regarding PsychrotrophicFoods (Basel, Switzerland) · 2025Review
- Support Enzyme Loading Influences the Effect of Aldehyde Dextran Modification on the Specificity of Immobilized Ficin for Large Proteins.Molecules (Basel, Switzerland) · 2024Article
- Cold-active microbial enzymes and their biotechnological applications.Microbial biotechnology · 2024Review
- Biochemical and in silico structural characterization of a cold-active arginase from the psychrophilic yeast, Glaciozyma antarctica PI12.Extremophiles : life under extreme conditions · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The modern biotechnology industry has a demand for macromolecules that can function in extreme environments. One example is cold-adapted proteases, possessing advantages such as maintaining high catalytic efficiency at low temperature and low energy input during production and inactivation. Meanwhile, cold-adapted proteases are characterised by sustainability, environmental protection, and energy conservation; therefore, they hold significant economic and ecological value regarding resource utilisation and the global biogeochemical cycle. Recently, the development and application of cold-adapted proteases have gained gaining increasing attention; however, their applications potential has not yet been fully developed, which has seriously restricted the promotion and application of cold-adapted proteases in the industry. This article introduces the source, related enzymology characteristics, cold resistance mechanism, and the structure-function relationship of cold-adapted proteases in detail. This is in addition to discussing related biotechnologies to improve stability, emphasise application potential in clinical medical research, and the constraints of the further developing of cold-adapted proteases. This article provides a reference for future research and the development of cold-adapted proteases.
Indexed as
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What OpenQuestion holds
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.