Background: Alchornea laxiflora (Benth.) Pax & K. Hoffm. (A. laxiflora) is utilized as a traditional herb for treating several diseases. Objective: Our study aims to identify the active phytochemical candidates from A. laxiflora and analyses to predict their anticancer activity mechanism by employing network pharmacology, molecular docking, and molecular dynamics (MD). Methods: The phytoconstituents of A. laxiflora were retrieved from the literature, and phytoconstituent-related targets implicated in hepatocellular carcinoma (HCC) were collected from respective databases. Computational methods were employed to recognize essential compounds, hub gene targets, and signaling pathways. Results: Our study has identified 12 potentially bioactive compounds, 150 potential anti-HCC targets, and 15 hub gene targets for A. laxiflora. Molecular docking results recognized the better binding energy values of below −5.6 kcal/mol. Further, MD simulations of the three of the top-scoring protein–ligand complexes (MAPK—3-acetylursolic acid, AKT1—quercetin, and AKT1—3-acetylursolic acid) allowed us to validate the docking results, evaluate the stability of the complexes, and associated conformational changes. Conclusions: Our research claims that phytoconstituents of A. laxiflora are crucial for treating liver cancer, and the recognized protein targets can serve as biomarkers, respectively.

Elimination of sugarcane grassy shoot disease (SGSD) through apical meristem culture technique for producing clean planting material of sugarcane has been attempted in the present study. The results showed that meristems length of 2 and 3 mm were free from the SGSD pathogen at higher frequency than larger meristem length of 4 mm. However, the frequency of survival of explants during initiation of shoot cultures was higher in larger meristems (60%) in comparison to smaller ones (40%). The micropropagated plantlets raised from meristem culture were confirmed for disease-free by nested polymerase chain reaction (PCR) analysis at monthly interval up to 6 months. This is the first report on the elimination of SGSD phytoplasma through meristem culture in India.

Introduction: Penicillin G amidase is an industrially significant enzyme widely employed in the production of semi-synthetic β-lactam antibiotics through the hydrolysis of Penicillin G to 6- aminopenicillanic acid. Owing to its commercial importance, extensive research has focused on improving the operational stability, reusability, and catalytic efficiency of PGA through various immobilization strategies. Methods: Optimization of multiple parameters for free and immobilized Penicillin G Acylase (PGA) is critical for improving the enzyme';s catalytic effectiveness, stability, and reusability in industrial and medicinal applications. This procedure entails methodically altering and analyzing variables such as substrate concentration, mechanical stability, cycle number, and storage conditions, and their effects on operational stability, pH, and temperature. PGA was optimized by entrapment on collagen hydrogel beads, resulting in collagen hydrogel + gelatin hybrid gel beads. Result: Immobilized PGA in Collagen Hydrogel + gelatin hybrid beads showed superior thermal stability, reusability, and storage stability as compared to gelatin-immobilized PGA. The entrapment of PGA onto Collagen Hydrogel + gelatin hybrid beads revealed several advantages and could be used in the production of 6-aminopenicillanic acid (6APA). Discussion: The study investigated the biochemical behavior of Penicillin G amidase (PGA) immobilized on collagen hydrogel and a collagen–gelatin bio-composite. Relative analysis focused on enzyme activity, stability, and mechanical strength, revealing insights into their appropriateness as immobilization matrices for enhanced PGA performance in industrial biocatalysis applications. Conclusion: Hydrogel + gelatin hybrid beads are more beneficial in industrial applications due to their greater stability and usability. PGA entrapment onto Hydrogel + gelatin hybrid beads has shown numerous advantages and may be useful in the manufacture of 6APA (6-aminopenicillanic acid).