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Mutanase (α‐1,3‐glucanase) is an inducible extracellular enzyme with potential medical applications in dentistry. A novel Cellulosimicrobium funkei strain SNG1 producing mutanase enzyme using α‐1,3‐glucans was isolated, and the enzyme was optimized for increased productivity using the one‐factor‐at‐a‐time approach. Maximum growth and enzyme‐specific activity (2.12 ± 0.4 U/mg) were attained in a production medium with pH 7.0 and 1% α‐1,3‐glucans as carbon source, incubated at 37°C for 30 h. The result showed a five‐fold increase in activity compared to unoptimized conditions (0.40 U/mg). The enzyme was purified by gel‐filtration chromatography, and recovered with a yield of 29.03% and a specific activity increase of 10.9‐fold. The molecular mass of the monomeric enzyme is 137 kDa. The pH and temperature optima are 6.0 and 45°C with Km of 1.28 ± 0.11 mg for α‐1,3‐glucans. The enzyme activity was stimulated by adding Co2+, Ca2+, Cu2+, and was entirely inhibited by Hg2+. On 2‐h incubation, the purified enzyme effectively degraded in vitro film with an 82.68% degradation rate and a saccharification yield of 30%.

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