All the 44 EHPs retrieved from the DEG database were considered for physicochemical characterization (Table ). Molecular weight plays an important role in the functional characterization of proteins. Protein Q5NFM6 and protein Q5NG09 showed the highest and lowest molecular weights of 52390.21 Da and 5897.62 Da, respectively. Isoelectric point (pI) prediction helps in the development of buffer systems and subsequent purification processes. The predicted pI value ranged from 4.21 to 9.77. Out of 44 EHPs, 23 were found to be acidic, having pI values ranging from 4.21 to 6.96 and 21 were found to be basic, having pI values ranging from 7.63 to 9.77. The extinction coefficient of the EHPs was estimated in water at 280 nm based on the concentration of cysteine, tryptophan, and tyrosine residues in the protein sequences . A higher percentage of these residues is responsible for higher extinction coefficient values. Calculation of the extinction coefficient helps in the quantitative analysis of protein-ligand and protein-protein interactions for drug discovery investigations. Protein Q5NFU0 and protein Q5NEJ2 were found to have the highest and lowest extinction coefficient values, respectively, whereas Q5NIM1 did not show the value due to the absence of cysteine, tryptophan, and tyrosine amino acid residues. The instability index indicates the stability of protein in the test tube environment . 16 proteins scored greater than 40 with a maximum score of 50.89 (Q5NFJ0) in the instability index and thus classified as unstable, whereas 28 proteins were confirmed to be stable, having the lowest score of 12.95 (Q5NHH0). Proteins with a higher aliphatic index usually show higher thermal stability . The aliphatic index values for the EHPs ranged from 48.89 (Q5NG09) to 156.01 (Q5NIL0). Grand average of hydropathicity (GRAVY) value elucidates protein-water interactions . Estimated GRAVY value ranged from -0.951 to 1.169 and showed 9 proteins to be hydrophobic and 35 proteins to be hydrophilic.