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In past several years, mannanases has attracted many researchers owing to its extensive industrial applications. The search for novel mannanases with high stability still continues. Present investigation was focused on purification of extracellular β-mannanase from Penicillium aculeatum APS1 and its characterization. APS1 mannanase was purified to homogeneity by chromatography techniques. Protein identification by MALDI-TOF MS/MS revealed that the enzyme belongs to GH family 5 and subfamily 7, and possesses CBM1. The molecular weight was found to be 40.6 kDa. The optimum temperature and pH of APS1 mannanase were 70 °C and 5.5, respectively. APS1 mannanase was found to be highly stable at 50 °C and tolerant at 55–60 °C. The enzyme was very sensitive to Mn⁺², Hg⁺² and Co⁺² metal ions and stimulated by Zn⁺². Inhibition of activity by N-bromosuccinimide suggested key role of …