ArticleMicrobial cell factories2026
Recombinant thermotolerant alkaline lipase from Lysinibacillus fusiformis for detergent and hard (Ras) cheese applications: cloning, expression, molecular docking, and characterization.
Article in Microbial cell factories, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
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
No grant is acknowledged in the PubMed record.
Abstract
backgroundThermostable and alkaline lipases are of significant interest for industrial applications, particularly in detergents and food processing. This study aimed to isolate, clone, and express lipase-encoding genes from a potent bacterial source to produce a thermo-tolerant alkaline lipase with enhanced catalytic efficiency and practical applicability.
resultsAmong several bacterial isolates, the most potent lipase producer was identified as Lysinibacillus fusiformis, and its 16 S rRNA sequence was deposited in GenBank (PP757498). Three lipase-encoding genes (est, est2, and lipA) were successfully isolated, cloned, and heterologously expressed in Escherichia coli BL21 (DE3). Their sequences were submitted to GenBank under accession numbers PX136937.1, PX136938.1, and PX136936.1, respectively. The recombinant lipase encoded by lipA (rLipase) exhibited the highest activity (150 U/mL) compared with the native enzyme (56.2 U/mL). Molecular docking analysis demonstrated strong binding affinity of rLipase toward major fatty acid derivatives in olive oil, with the highest affinity for linoleic acid (- 8.0 kcal/mol), followed by oleic acid (- 7.8 kcal/mol) and palmitic acid (- 7.3 kcal/mol). These interactions were stabilized by hydrophobic interactions and hydrogen bonding, with key contributions from critical amino acid residues, particularly VAL250. The partially purified recombinant lipase (rLipase) exhibited a maximum activity of 320 U/mL at 80 °C and pH 9, demonstrating remarkable thermostability and alkaline tolerance. Functional evaluation showed that rLipase improved the detergent efficiency for oil stain-removal from cotton fabrics. In addition, supplementation with 0.4% rLipase accelerated Ras cheese ripening by shortening the maturation period from 120 to 90 days with maintaining the desired ripening process.
conclusionsThe recombinant lipase from Lysinibacillus fusiformis demonstrated high thermal stability, alkaline tolerance, and strong catalytic efficiency. Its effectiveness in detergent formulations and cheese ripening highlights its potential as a versatile industrial biocatalyst for lipid bioconversion and related applications.
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.