Liu N, Zhang T, Wang Y J, Huang Y P, Ou J H, Shen P
College of Life Sciences, Wuhan University, Wuhan, China.
Lett Appl Microbiol. 2004;39(5):407-12. doi: 10.1111/j.1472-765X.2004.01599.x.
The objective of this work was to purify the tyrosinase from Bacillusthuringiensis subsp. kurstaki (Bt) (CCTCC AB 90010) and study its enzymatic properties.
A 'one-step' purification method was used in this work, which was an easy, high-yield purification method. Tyrosinase activity of this purity was measured under different conditions to study its kinetic characterizations. The optimum pH and thermal stability of this enzyme were also determined. The results revealed that the tyrosinase from Bt has distinct properties compared with those from other sources.
A heat-inducible tyrosinase of a wild strain of Bt was identified and partially characterized.
The distinct properties of Bt tyrosinase are important to the application of Bt as a biology pesticide.
本研究旨在从苏云金芽孢杆菌库斯塔克亚种(Bt)(中国典型培养物保藏中心保藏编号AB 90010)中纯化酪氨酸酶,并研究其酶学性质。
本研究采用“一步法”纯化方法,该方法简便且产率高。在不同条件下测定该纯度的酪氨酸酶活性,以研究其动力学特征。还测定了该酶的最适pH值和热稳定性。结果表明,Bt来源的酪氨酸酶与其他来源的酪氨酸酶具有不同的性质。
鉴定了一株Bt野生菌株的热诱导型酪氨酸酶,并对其进行了部分特性表征。
Bt酪氨酸酶的独特性质对Bt作为生物农药的应用具有重要意义。