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Mannanase is the main enzyme that catalyzes depolymerization of -1,4 mannosidic linkages within the main chain of mannan releasing manno-oligosacharides.Since mannan is most soluble at alkaline solution and industrial enzymes application prefer high thermostability, therefore mannanase with alkaline and high thermostability is more desired. This aim of this study is to isolate mannase-producing microorganisms and to characterize mannanase that obtained from partial purification. Nine mannolytic isolates were found and the chosen isolate was R11 with mannolytic index of 3,287. The purity enzyme from partial purification was 6,06 fold with the specific activity 61,54 U/mg. Molecular mass of the mannanase analyzed by electhrophoresis and zymogram was 32,39 kDa. The optimal temperatures and pH were 65oC and pH 8, repectively. The enzyme was stable at pH 5 – 8 and temperatures up to 75oC. This properties makes mannanase R311 is attractive for biotechnological application for industries.