|
|||||
|
|
| 非离子表面活性剂存在下过氧化氢对木素过氧化物酶的抑制动力学研究 | |
| 引用本文： | 王丹,黄锡荣,宋少芳,于专妮,卢雪梅,曲音波,高培基.非离子表面活性剂存在下过氧化氢对木素过氧化物酶的抑制动力学研究[J].山东大学学报(理学版),2003,38(2):108-111. |
| 作者姓名： | 王丹 黄锡荣 宋少芳 于专妮 卢雪梅 曲音波 高培基 |
| 作者单位： | 1. 山东大学,胶体与界面化学教育部重点实验室,山东,济南,250100 2. 山东大学,胶体与界面化学教育部重点实验室,山东,济南,250100;山东大学,微生物技术国家重点实验室,山东,济南,250100 3. 山东大学,微生物技术国家重点实验室,山东,济南,250100 |
| 基金项目： | 教育部高等学校重点实验室访问学者基金，山东省自然科学基金(Y2 0 0 0D11)，国家自然科学基金(2 990 60 0 5 )资助项目 |
| 摘 要： | 研究表面活性剂水溶液体系中木素模型化合物的酶法降解机制具有重要意义．本文用动力光度技术研究了非离子表面活性剂TritonX-100(TNX)存在下过氧化氢对木素过氧化物酶(LiP)的抑制作用．结果表明，该抑制作用属可逆竞争抑制．TNX的存在使H2O2的抑制作用加强，抑制常数Ki值下降．Ki值随TNX浓度(远低于、接近于和远大于其临界胶束浓度)变化很小这一结果表明起主导作用的是TNX单体，上述结果应该是有限数目的表面活性剂单体对酶蛋白分子的修饰所致． |
| 关 键 词： | 木素过氧化物酶 过氧化氢 非离子表面活性剂 抑制动力学 藜芦醇 降解机制 动力光度技术 |
| 文章编号： | 1671-9352(2003)02-0108-04 |
| 修稿时间： | 2002年9月24日 |
Kinetic Studies on The Inhibition of Ligninase By Hydrogen Peroxide in the Presence of Nonionic Surfactant |
|
| WANG Dan ,HUANG Xi rong ,SONG Shao fang ,YU Zhuan ni ,LU Xue mei ,QU Yin bo & GAO Pei ji.Kinetic Studies on The Inhibition of Ligninase By Hydrogen Peroxide in the Presence of Nonionic Surfactant[J].Journal of Shandong University,2003,38(2):108-111. | |
| Authors: | WANG Dan HUANG Xi rong SONG Shao fang YU Zhuan ni LU Xue mei QU Yin bo & GAO Pei ji |
| Institution: | WANG Dan 1,HUANG Xi rong 1,2*,SONG Shao fang 1,YU Zhuan ni 1,LU Xue mei 2,QU Yin bo 2 & GAO Pei ji 2 |
| Abstract: | Studies of biodegradation of lignin model compounds by enzyme in aqueous media containing surfactant is of great significance to the world's environment and resources. In this paper, the inhibition of ligninase (LiP) by hydrogen peroxide in the presence of nonionic surfactant TritonX 100 has been investigated using kinetic spectrophotometric technique. Based on the results of kinetic studies of the ligninase catalyzed oxidation of veratryl alcohol (VA) by H 2O 2 , a reversible competitive pattern of inhibition is suggested. Presence of TritonX 100 enhances the inhibition by H 2O 2 and, therefore, causes the inhibition constant Ki to decrease. Based on the fact that Ki changes little with the concentrations of TritonX 100 (lower than, near to, and larger than its critical micelle concentration), it may be concluded that the monomer of TritonX 100, maybe through its modification to the enzymic protein, is responsible for the above mentioned results. |
| Keywords: | ligninase hydrogen peroxide non ionic surfactant inhibitory kinetics veratryl alcohol |
| 本文献已被 CNKI 维普 万方数据 等数据库收录！ | |