Irpex lacteus dft-1漆酶在反胶束中的催化性能研究  

Catalytic Performance of Laccase of Irpex lacteus dft-1 in Reverse Micelles

作　　者：姬广磊[1] 

机构地区：[1]山东大学环境科学与工程学院,山东济南250100

出　　处：《环境科学与技术》2009年第12期79-84,共6页Environmental Science & Technology

摘　　要：对酶工程而言,在反应体系中保持较高的酶的活性和稳定性是取得较高酶催化效率的关键。文章考察了不同参数,即含水量W0、缓冲液的种类、pH和离子强度、AOT浓度和酶浓度对Irpex lacteusdft-1漆酶在AOT/异辛烷反胶束中的催化活性和稳定性的影响。结果表明,酶活性随W0的增大而提高,当W0>35,其活性不再有明显的变化,而其稳定性在较小的W0下较好。酶的最佳反应pH为4.2,但稳定性随pH的升高而增强。在较小表面活性剂浓度下,酶活性和稳定性较高,随着表面活性剂浓度的提高,酶活性和稳定性下降。不同的缓冲液体系对酶的活性和稳定性影响不同,酶活性随缓冲液离子强度提高先升高而后下降,而酶在较小的离子强度下具有较好的稳定性。酶浓度升高其活性提高,但对酶的稳定性没有明显的影响。Enzyme activity and stability are critical factors for enzyme engineering to achieve higher catalytic efficiency. The effect of various parameters including water content, pH, buffer composition and ionic strength, concentration of AOT and enzyme on activity and stability of laccase isolated and purified from Irpex lacteus dft-1 in AOT/isooctane were investigated. It was found that enzyme activity was increased with increase of water content and it was no longer change significantly when water content exceeded 35, but enzyme stability was better at lower water content. The optimum pH for enzyme reaction was 4.2 whereas the enzyme stability was increased with increase of pH. The enzyme activity and stability were both decreased with increase of concentration of AOT. The enzyme activity and stability were different with various buffer media. The enzyme activity was first increased then decreased with increase of buffer ionic strength whereas the enzyme stability was better at lower ionic strength. With the increase of enzyme concentration, the enzyme activity increased, but it had no significant effect on enzyme stability.

关 键 词：漆酶 反胶束 酶活性 酶稳定性 

分 类 号：X172[环境科学与工程—环境科学]