ReviewJournal of food science2026
Lipase Stability in Structured Lipid Synthesis: The Interplay of Substrate Characteristics and Strategies to Improve Its Operational Performance-A Critical Review.
Review in Journal of food science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
1 citing paper in PubMed.
- Enzymatic Synthesis of Lysophosphatidylcholine Containing γ-Linolenic and Stearidonic Acids in a Solvent-Free System.Foods (Basel, Switzerland) · 2026Article
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.
Funding
Abstract
Structured lipids (SLs) have attracted growing industrial interest due to their associated health benefits. Lipases, as highly selective and versatile biocatalysts, are central to the sustainable synthesis of SLs attributed to their ability to operate under mild reaction conditions. However, the limited operational stability of lipases remains a major bottleneck, directly affecting process efficiency, product yield, and economic feasibility. While considerable attention has been devoted to enzyme engineering and process optimization, the influence of lipid substrate characteristics on lipase stability has received comparatively little scrutiny. This review critically examines feedstock properties, such as oxidative status, free fatty acid composition, and water activity, that affect lipase performance and deactivation during SL synthesis, where unoptimized substrate characteristics have been shown to reduce lipase stability by two- to sevenfold. It further discusses mitigation strategies, including substrate pretreatment with protein, adsorbents, and antioxidant, as well as process design enhancements, which have demonstrated up to sevenfold extensions in operational stability. This review highlights the importance of integrating substrate quality management into biocatalytic process design to enhance lipase operational stability and reusability. By elucidating the interplay between substrate properties and enzyme stability, this work provides a foundation to promote the valorization of nontraditional lipid sources, such as agro-industry by-products and underutilized oils, within circular bioeconomy frameworks, thereby supporting the development of more flexible, robust, cost-effective, and scalable biocatalytic processes for SL production.
Indexed as
Identifiers
What Socratic 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 Socratic graph.