N-Carbamoyl-amino acidamidohydrolase 基因已從Bacilluskaustophilus 中被選殖出來，並在Escherichia coli 菌體中表現，之後純化N-carbamoylase 酵素，探討其酵素特性，發現Mn2+、Co2+或Ni2+離子存在時提高酵素活性到6 倍，而Cu2+離子則不會抑制酵素活性。此Nca 對H2 O2的氧化作用有很差的抗性，且不受NH4+的回饋抑制。酵素的最適反應pH 及溫度分別為7.4 及70 ℃。在酵素中添加D 型或L 型基質，於50 ℃中保溫36 天，完全沒失去活性。B.kaustophilus 的N-carbamoylase 能將N-Carbamoyl-L-amino acids 轉換成對應的胺基酸至於基質如N-Carbamoyl-D 型衍生物沒有活性。
N-Carbamoyl-amino acid amidohydrolase gene from Bacillus kaustophilus was cloned and expressed in Escherichia coli. N-Carbamoylase was purified by immobilized metal affinity thromatography. The enzyme activity was elveated by Mn 2+ ，Co 2+ or Ni 2+ ions to 6 folds but not inhibited by Cu 2+ ion.The enzyme was sensitive to H2 O2 oxidation but resistant to NH4 + inhibition.The optimal pH and temperature for the catalytic activity were7.4 and 70 ℃，respectively.After incubation at 50 ℃for 36 days no enzyme activity was lost in a reaction mixture containing D formed or L specific substrates.B. kaustophilus N-carbamoylase is cable of converting N-Carbamoyl-L-amino acids to corresponding amino acids ，rest of substrates such as N-Carbamoyl-D-derivatives were not hydrolyed.
