Purification and Molecular Mass of β-Glucosidase
The BGL from Phoma sp. KCTC11825BP was purified 8.5-fold with a 34.3% yield and a final specific activity of 84.5 U/mg with pNPG as substrate (Table 1).
Proteins obtained at each purification step were analyzed by SDS-PAGE and the final purified enzyme showed a single band
with a molecular mass of approximately 110 kDa (Fig. 2A).
The native enzyme existed as a tetramer with a molecular mass of 440 kDa (Fig. 2B). This BGL had a higher molecular
mass and was more multimeric than the well-known BGL in nature [6, 22].