Syncephalastrum racemosum RR 96, MTCC 2774, synthesized extra-cellular β-amylase (EC 3.2.1.2) when cultivated with starch as sole carbon source. The strain showed maximum β-amylolytic activity on the fourth day of cultivation, and the partly purified enzyme showed highest activity at 60° and pH 5. About 60% of the activity was found to be retained within the range pH 4–7. The enzyme activity was not increased in presence of exogenous thiols and remained unaffected in presence of heavy metals and the thiol inhibitor p-chloromercuribenzoate, indicating the absence of thiols at the active site of the enzyme. Absence of substrate cross specificity and ability to hydrolyse waste starches made the enzyme competent for industrial application.