An inducible and heterocyclic thermostable nitrilase was obtained from Staphylococcus sp. KP789135.1. The whole cell nitrilase was active at 50 °C temperature and neutral pH with a half-life of 4 h at 50 °C and 2.5 h at 60 °C. Metal ions such as Fe³⁺, Mg²⁺, and Ca²⁺ enhanced the biocatalytic activity while Ag²⁺, Hg²⁺, and Cu²⁺ completely inhibited biocatalysis, which confirmed the presence of thiol group in the catalytic site. Staphylococcus sp. KP789135.1 has broad hydrolytic activity towards heterocyclic nitriles and few amides. It showed high tolerance against 3-cyanopyridine (5 mM - 20 mM). The calculated Km and Vmax were 1.33 mM and 0.98 U, lower km values demonstrated the highest affinity towards 3-cyanopyridine. In silico study revealed 99% similarity with Staphylococcus strain. The 3D structures were deduced from I-TASSER server and validated from PROCHECK, found relatively low % of amino acid residues has phi/psi angles in the disallowed region that suggest the acceptability of Ramachandran plot in the present work. Docking study revealed 3-cyanopyridine has lowest potential energy (potential energy OPLS -7.00745) and thus showed more stable enzyme ligand interaction. This is the first report on biotransformation of 3-cyanopyridine to nicotinic acid using thermostable nitrilase from Staphylococcus sp.

从葡萄球菌获得了可诱导的杂环热稳定腈水解酶。KP789135.1。全细胞腈水解酶在50°C的温度和中性pH下具有活性，在50°C的半衰期为4 h，在60°C的半衰期为2.5 h。Fe ³⁺，Mg ²⁺和Ca ²⁺等金属离子增强了生物催化活性，而Ag 2 ⁺，Hg ²⁺和Cu ^2+则完全抑制了生物催化作用，证实了催化位点中存在巯基。葡萄球菌sp。KP789135.1具有对杂环腈和少量酰胺的广泛水解活性。它显示出对3-氰基吡啶的高耐受性（5 mM-20 mM）。计算得出的Km和Vmax为1.33 mM和0.98 U，较低的km值表明对3-氰基吡啶的亲和力最高。在计算机研究中发现与葡萄球菌有99％的相似性应变。从I-TASSER服务器推导并通过PROCHECK验证了3D结构，发现相对较低百分比的氨基酸残基在不允许的区域中具有phi / psi角，这表明Ramachandran图在本研究中是可接受的。对接研究表明3-氰基吡啶具有最低的势能（势能OPLS -7.00745），因此显示出更稳定的酶配体相互作用。这是关于使用葡萄球菌属的热稳定腈水解酶将3-氰基吡啶生物转化为烟酸的首次报道。