ReviewMicroorganisms2021
Microbial L-asparaginase for Application in Acrylamide Mitigation from Food: Current Research Status and Future Perspectives.
Review in Microorganisms, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed, 117 citations in OpenAlex.
- Fusion Protein Technology to Enhance Pharmacological Properties of L-Asparaginases.Biomolecules · 2026Review
- Biochemical characterisation of a new thermotolerant L-asparaginase produced by Cunninghamella echinulata PA3S12MM isolated from the Atlantic Forest.Archives of microbiology · 2026Article
- Efficient production of L-asparaginase using recombinant Pichia pastoris and strategy to eliminate glutaminase activity.Biotechnology letters · 2026Article
- The Asparaginase Database: a comprehensive resource and classification of l-asparaginases.Database : the journal of biological databases and curation · 2026Article
- Production of L-asparaginase from Candida utilis by solid-state fermentation: a comprehensive assessment of its antiproliferative potential on glioblastoma cells.World journal of microbiology & biotechnology · 2025Article
- Secretory Expression ofJournal of microbiology and biotechnology · 2025Article
- Characterization and bioactivities of glutaminase-free L-asparaginase from Salinicola acorporae S4-41.Microbial cell factories · 2025Article
- L-asparaginase: a review of microbial production and protein engineering with translational applications for oncology and food safety.World journal of microbiology & biotechnology · 2025Review
- Acrylamide and Advanced Glycation End Products in Frying Food: Formation, Effects, and Harmfulness.Foods (Basel, Switzerland) · 2025Review
- Algal L- asparaginase: Antioxidant activity, mitigation of acrylamide in fried potato chips, sensory quality and immobilization.Journal, genetic engineering & biotechnology · 2025Article
- Evaluation of the effect of enzymatic pretreatment with l-asparaginase on acrylamide formation during microwave, air, and deep frying of potatoes.Journal of food science · 2025Article
- Marine-derived L-asparaginase: unlocking marine power in anti-tumor therapeutics.Frontiers in immunology · 2025Review
- Recent advances in L-Asparaginase enzyme production and formulation development for acrylamide reduction during food processing.Food chemistry: X · 2025Review
- Exploring Bioactive Potential ofIndian journal of microbiology · 2024Article
- L-Asparaginase Conjugates from the Hyperthermophilic ArchaeaInternational journal of molecular sciences · 2024Article
- Dietary Acrylamide: A Detailed Review on Formation, Detection, Mitigation, and Its Health Impacts.Foods (Basel, Switzerland) · 2024Review
- Cloning, expression, and characterization of a novel thermo-acidophilic l-asparaginase of3 Biotech · 2024Article
- A Comprehensive Review of the Diversity of Fungal Secondary Metabolites and Their Emerging Applications in Healthcare and Environment.Mycobiology · 2024Review
- Thermal Stability Enhancement of L-Asparaginase fromFoods (Basel, Switzerland) · 2023Article
- Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production.International journal of molecular sciences · 2023Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
L-asparaginase (E.C.3.5.1.1) hydrolyzes L-asparagine to L-aspartic acid and ammonia, which has been widely applied in the pharmaceutical and food industries. Microbes have advantages for L-asparaginase production, and there are several commercially available forms of L-asparaginase, all of which are derived from microbes. Generally, L-asparaginase has an optimum pH range of 5.0-9.0 and an optimum temperature of between 30 and 60 °C. However, the optimum temperature of L-asparaginase from hyperthermophilic archaea is considerable higher (between 85 and 100 °C). The native properties of the enzymes can be enhanced by using immobilization techniques. The stability and recyclability of immobilized enzymes makes them more suitable for food applications. This current work describes the classification, catalytic mechanism, production, purification, and immobilization of microbial L-asparaginase, focusing on its application as an effective reducer of acrylamide in fried potato products, bakery products, and coffee. This highlights the prospects of cost-effective L-asparaginase, thermostable L-asparaginase, and immobilized L-asparaginase as good candidates for food application in the future.
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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.