A gene encoding chitin deacetylase from Bacillus cereus M1(BcCDA) was obtained. BcCDA was re-combinant expressed in Escherichia coli at the secretion form and purified by affinity chromotagraphy.The purity of the purified BcCDA was tested by SDS-PAGE, which molecular weight was approximately 23 kD.The re-combinant BcCDA had deacetylase activity, which specific activity was 11 608.31 U/mg. The research would provide a basis for studying the action mechnism and harness of BcCDA.%从产几丁质脱乙酰基酶的蜡状芽孢杆菌（Bacillus cereus M1）中获得了几丁质脱乙酰基酶BcCDA基因序列，并在大肠杆菌中实现了其高效分泌表达以及一步亲和法纯化重组几丁质脱乙酰基酶BcCDA，经SDS-PAGE检测该酶为单一条带，其分子量约为23 kD，所得重组BcCDA的具有脱乙酰基酶活性，其比活力为11608.31 U/mg。该研究为BcCDA作用机制的进一步研究和BcCDA的利用鉴定基础。
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