对鸡毛高效降解Deinococcus sp. RM菌株的基因组，及其降解鸡毛过程中的转录组进行测序，筛选出表达量高的蛋白酶基因重组至Pichia pastoris GS115菌株中进行诱导表达，对重组蛋白酶分离纯化、酶学性质以及降解鸡毛的效果进行测定。结果表明，RM菌株共4 132个基因，3 844个基因表达，其中444个基因表达胞外蛋白，26个为胞外蛋白酶。较高表达量的sp02200基因在P. pastoris GS115菌株中获得成功表达，该重组蛋白酶rSp02200属于一种新型热应激需求蛋白家族DegQ类蛋白酶，最适反应温度为37 ℃，在30 ℃以下保持较好稳定性，最适pH 为7.5，在pH 4.0~11.0能保持70%以上蛋白酶活性，并且能将长、粗的鸡毛羽轴和羽枝降解为细小的羽轴和羽枝。因此，Sp02200蛋白酶是RM菌株降解鸡毛过程中的一种重要酶，这为探究RM菌株降解鸡毛相关基因的研究提供了参考。

The genome of Deinococcus sp. RM strain and its transcriptome in the process of chicken feather degradation were sequenced, the protease gene with high expression was selected and recombined in Pichia pastoris GS115 strain for induction expression. The purification, enzymatic properties and the effects of chicken feather degradation of the recombinant protease were determined. The results showed that RM strain had 4 132 genes and 3 844 genes expressed, of which 444 genes expressed extracellular proteins and 26 were extracellular proteases. The high expression gene sp02200 was successfully expressed in the P. pastoris GS115 strain. The recombinant protease rSp02200 belonged to a novel DegQ protease of high-temperature requirement family, with an optimal reaction temperature of 37 ℃, and remained good stability below 30 ℃. The optimal pH was 7.5, and maintained more than 70% protease activity at pH 4.0-11.0. The protease can degrade long and thick feather axes and branches into small feather axes and branches. Therefore, Sp02200 protease was an important protease in the chicken feather degradation process of RM strain, which provides a reference for exploring related genes involved in feather degradation of RM strain.