Thermostable 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. Among 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. The 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.
G. El-Sayed, Hala R. Wehaidy, A. Kholif et al.· Microbial Cell Factories· 0 citations
The fall armyworm (S. frugiperda) has developed resistance to numerous insecticides and is currently considered one of the most destructive pests threatening global crop production. Consequently, the development of environmentally sustainable pest management strategies has become increasingly important. Insect-associated pathogenic bacteria represent a promising source of bioactive metabolites with potential insecticidal properties. In the present study, pathogenic bacteria associated with S. frugiperda were isolated and molecularly identified as Serratia marcescens strain INS420 based on 16 S rRNA gene sequencing. The secondary metabolites produced by this bacterium demonstrated significant insecticidal activity under both laboratory and field conditions. Metabolic profiling of the extracted compounds was performed using liquid chromatography–mass spectrometry (LC–MS) and gas chromatography–mass spectrometry (GC–MS), revealing the presence of several bioactive compounds, including diketopiperazines, fatty acids and their esters, squalene, phthalate derivatives, and a cardenolide. To gain insights into the potential mechanism of action, molecular docking simulations were conducted to evaluate the binding affinity of the identified metabolites with S. frugiperda acetylcholinesterase (AChE). Among the detected compounds, squalene and several fatty acid derivatives exhibited stable interactions within the active site of the enzyme, suggesting a possible inhibitory effect on AChE activity. Collectively, these findings demonstrate that S. marcescens associated with S. frugiperda produces metabolites with notable insecticidal potential and highlight insect-associated pathogenic bacteria as a valuable source of bioactive compounds for the sustainable management of fall armyworm.
Kreema A. El-Lebody, Ramy E. El-Ansary, Shaimaa A. Nour et al.· Scientific Reports· 0 citations
This research provides the first extensive breed‑pool whole‑genome sequencing (WGS) analysis across five Egyptian sheep populations, establishing a genomic atlas for the genetic architecture of production and adaptation in Egyptian sheep, providing a baseline for future genetic and conservation strategies.
Nada N A M Hassanine, Ali H. Amin, E. Hafez et al.· BMC Biotechnology· 0 citations
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