Acta Chimica Sinica ›› 2005, Vol. 63 ›› Issue (21): 2009-2012. Previous Articles     Next Articles

Reports

直链醇对反胶束体系中木素过氧化物酶催化活性的影响

张文娟1,王丹1,黄锡荣*,1,2,曲音波2,高培基2   

  1. (1山东大学胶体与界面化学教育部重点实验室 2微生物技术国家重点实验室 济南 250100)
  • 收稿日期:2005-01-27 修回日期:2005-07-07 出版日期:2005-11-14 发布日期:2010-12-10
  • 通讯作者: 黄锡荣

Effects of Normal Alcohols on the Catalytic Activity of Lignin Peroxidase in Reversed Micelles

ZHANG Wen-Juan1, WANG Dan1, HUANG Xi-Rong*,1,2, QU Yin-Bo2, GAO Pei-Ji2   

  1. (1 Key Laboratory of Colloid and Interface Chemistry of the Ministry of Education of China, 2State Key Laboratory of
    Microbial Technology, Shandong University, Jinan 250100)
  • Received:2005-01-27 Revised:2005-07-07 Online:2005-11-14 Published:2010-12-10
  • Contact: HUANG Xi-Rong

Previous studies indicated that lignin peroxidase (LiP) hosted at CTAB/n-alcohol/isooctane/water reversed micelle did not show any catalytic activity, but in normal micellar solution of CTAB, LiP could express its catalytic activity. To reveal the role of normal alcohol, the effects of the alcohol with different carbon chain length on the catalytic activity of LiP were investigated. Because the content of the alcohol in the CTAB reversed micellar medium was high and the normal alcohols with the number of carbon atoms higher than 4 were slightly soluble in water, three media in which LiP could express its catalytic activity, i.e., a CTAB normal micellar medium, an AOT reversed micellar medium, and a Brij 30 reversed micellar medium, were used to study the effect of normal alcohols on the catalytic activity of LiP. Results indicated that as long as the concentration of the alcohol exceeded 500 mmol•L-1 (≥1200 mmol•L-1 for butanol), LiP lost its activity completely in the three media above regardless of the structure, the electrical property and the size of the surfactant aggregates. Consequently it was deduced that the phenomenon that LiP hosted at CTAB reversed micelles could not express its activity was mainly due to the alcohol co-surfactant.

Key words: lignin peroxidase, normal alcohol, reversed micelle, catalytic activity