• 何小慧,刘幽燕,贺锴,李昂,覃益民.黄曲霉A5p1脱色类黑精及其机理初探:葡萄糖氧化酶的作用[J].环境科学学报,2014,34(12):3036-3042

  • 黄曲霉A5p1脱色类黑精及其机理初探:葡萄糖氧化酶的作用
  • Decolorization mechanism of melanoidin by Aspergillus flavus A5p1: the function of glucose oxidase
  • 基金项目:国家自然科学基金项目(No.21066001)
  • 作者
  • 单位
  • 何小慧
  • 广西大学化学化工学院, 南宁 530004
  • 刘幽燕
  • 1. 广西大学化学化工学院, 南宁 530004;2. 广西生物炼制重点实验室, 南宁 530003
  • 贺锴
  • 广西大学化学化工学院, 南宁 530004
  • 李昂
  • 广西大学化学化工学院, 南宁 530004
  • 覃益民
  • 广西大学化学化工学院, 南宁 530004
  • 摘要:类黑精是一种高分子难降解色素污染物质,在糖蜜酒精废水中大量存在.选取在前期研究中对糖蜜酒精废水具有较好脱色作用的黄曲霉(Aspergillus flavus)A5p1(保藏号CGMCC.4292),以合成的类黑精为对象研究脱色机理,试图为实际废水的生物脱色提供理论基础.结果显示,此菌株对合成类黑精具有生物吸附和生物降解的双重作用,以后者为主,最高脱色率可达65%.相较于漆酶、依赖/不依赖于锰的过氧化物酶等常规氧化脱色酶,此菌株中的产过氧化氢酶对脱色起主要作用,而且脱色过程中作为产过氧化氢酶之一的葡萄糖氧化酶与类黑精脱色率之间存在着一定的正相关性.添加葡萄糖氧化酶激活剂和抑制剂进行验证,发现葡萄糖氧化酶酶活力、过氧化氢产量和脱色率三者之间呈相关性变化.初步推测,葡萄糖氧化酶是黄曲霉A5p1生物降解脱色类黑精的关键酶之一.
  • Abstract:Melanoidin, a polymeric pollutant and hardly degradable pigment, presents largely in molasses wastewater. Since Aspergillus flavus A5p1(CGMCC No. 4292) showed a good ability in the decolorization of molasses wastewater, it was used as an object to investigate the decolorization mechanism of synthetic melanoidin, providing a theoretical basis for the bio-decolorization of melanoidin contained in wastewater. The results showed that synthetic melanoidin was decolored to 65% by Aspergillus flavus A5p1. There might be a synergistic effect of bio-adsorption and biodegradation on the decolorization. However, the biodegradation might play a more important role in the process. Compared to normal oxidative enzymes, such as Lac, MIP and MnP, H2O2-producing enzymes performed a main effect on decolorization. Glucose oxidase, one of H2O2-producing enzymes, generated a positive correlation with decolorization of melanoidin by Aspergillus flavus A5p1. By adding activator and inhibitor, the changes of the three parameters (activity of glucose oxidase, H2O2 production rate and decolorization rate) were positively correlated. It was suggested that the glucose oxidase, produced by Aspergillus flavus A5p1, was a key enzyme in the decolorization of melanoidin.

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