Biodiversity- Driven Study of Endophytic Fungi: Growth Parameters and Enzyme Production

The genus Miliusa comprises several species distributed across South and Southeast Asia, primarily in evergreen and semi evergreen forest ecosystems. Miliusa velutina contributes to forest biodiversity and plays a role in trophic interactions particularly in seed dispersal mechanisms. Its occurrence in tropical regions of India suggests potential relevance in ethnobotanical practices. Miliusa velutina is a medicinally significant plant valued for its traditional uses and diverse bioactive constituents. In traditional medicinal systems, especially in regions of India and Southeast Asia related Miliusa species have been used for managing infections, inflammation, and certain chronic conditions.

The objective of this work was to study the diversity of endophytic fungi and quantification of the enzymes in Miliusa velutina var deviyarina.

The plant was collected from its natural habitat in Maharashtra, India. Dominant taxa were identified based on relative abundance and classified as primary or secondary dominant taxa. Endophytic fungal isolates representing these taxa were recovered from surface sterilized tissues using Potato Dextrose Agar and Sabouraud’s Dextrose Agar, identified by ITS sequencing and cultured on different media for subsequent analyses.

Growth studies of the dominant fungal isolates demonstrated optimal growth at pH 6.5–7.0 and a temperature of 26 °-37 °C. Among the carbon sources evaluated, sucrose and fructose were identified as the most favourable, indicating the significant influence of environmental and nutritional parameters on fungal growth and metabolic activity.

The primary dominant endophytic fungi were identified as Aspergillus niger Tiegh., Colletotrichum siamense Prihast., Diaporthe sp. while the secondary dominant isolates included Lasiodiplodia mahajangana, Aspergillus tamarii and Phyllosticta capitalensis.

Enzymatic profiling revealed substantial production of extracellular enzymes including lipase (13.1 U/mL), esterase (18.7 U/mL), laccase (4.0 U/mL) and pectinase (8.5 U/mL). These results underscore the pronounced catalytic efficiency of the isolates and highlight their potential applicability in various biotechnological and industrial processes.