SM‐1‐TA and SM‐2‐TA: Heterologous Expression, Enzymatic/Structural Characterization, and Functional Complementarity of Two Tannase Isoenzymes From <i>Streptomyces avermitilis</i>

, respectively. Molecular dynamics (MD) simulations suggested that the lower thermal stability of SM-1-TA may originate from its higher overall flexibility and pronounced local fluctuations within the residue region 100-150. The functional complementarity between SM‑1‑TA and SM‑2‑TA observed in this study highlights the ecological significance of isoenzymes in microbial adaptation to diverse environments. These findings not only provide insights into the functional divergence of isoenzymes but also establish a foundation for the future discovery and engineering of tannases with enhanced properties.