Published Paper Details:

Halophilic actinomycetes are valuable sources of extremozymes with significant industrial potential due to their Sustain ability and function under high salinity and other harsh conditions. In this study, we conducted comprehensive bioinformatics-based structural and functional analysis on four amylase sequences from the halophilic actinomycetes Actinopolyspora erythraea, including ?-glucosidase, glycosidase and two hypothetical proteins. We retrieved four amino acid sequences from the NCBI database. Sequences were analysed by using ProtParam to determine physicochemical properties associated with halophilic adaptation. Three-dimensional structures were predicted using SWISS-MODEL and validated through Global Model Quality Estimation (GMQE), QMEAN Z-score, MolProbity and Ramachandran plot to capture the novelty of amylases. All analysed proteins exhibited hallmark features of halophilic enzymes, including low theoretical isoelectric points, enrichment of acidic amino acids, negative GRAVY values indicating enhanced hydrophilicity, and moderate to high aliphatic indices suggestive of thermostability. The ?-glucosidase and glycosidase proteins demonstrated favourable stability indices and structural robustness, supporting their primary roles in carbohydrate metabolism under hypersaline conditions. Overall, this study highlights key molecular determinants underlying halophilic adaptation in amylase-related proteins from Actinopolyspora erythraea and underscores the biotechnological potential of halophilic actinomycetes as promising sources of salt-tolerant enzymes for applications in the food, detergent, and pharmaceutical industries.