云芝
锰过氧化物酶
生物修复
化学
锰
核化学
基质(化学分析)
催化作用
过氧化物酶
流出物
固定化酶
色谱法
有机化学
漆酶
酶
废物管理
污染
生态学
工程类
生物
作者
Hafiz M.N. Iqbal,Muhammad Asgher
出处
期刊:Protein and Peptide Letters
[Bentham Science Publishers]
日期:2013-03-01
卷期号:20 (5): 591-600
被引量:56
标识
DOI:10.2174/0929866511320050013
摘要
A novel manganese peroxidase (MnP) isolated from solid state culture of Trametes versicolor IBL-04 was immobilized using xerogel matrix composed of trimethoxysilane (TMOS) and propyltetramethoxysilane (PTMS). FTIR spectroscopy confirmed the successful entrapment of MnP into the xerogel matrix. An immobilization efficiency of 92.2% was achieved with a purified active fraction containing 2 mg/mL MnP. After 24 h incubation at varying pH and temperatures, the immobilized MnP retained 82 and 75% activity at pH 4 and 80°C, respectively. Xerogel matrix immobilization enhanced the catalytic efficiency of entrapped MnP. Metal ions including Cu2+, Mn2+ and Fe2+ stimulated enzyme activity while cysteine, EDTA and Ag+ inhibited the activity. MnP preserved 82% of its initial activity during oxidation of MnSO4 in 10 consecutive cycles, demonstrating the reusability of xerogel entrapped MnP. The immobilized MnP could be stored for up to 75 days at 4°C without significant activity loss. To explore the industrial applicability of MnP, the immobilized MnP was tested for decolorization of textile industry effluent in a Packed Bed Reactor System (PBRS). After five consecutive cycles, 98.8% decolorization of effluent was achieved within 5 h. The kinetic properties, storage stability and reusability of entrapped MnP from T. versocolor IBL-04 reflect its prospects as biocatalyst for bioremediation and other industrial applications. Keywords: Bioremediation, characterization, immobilization, manganese peroxidase, T. versicolor IBL-04, characterization
科研通智能强力驱动
Strongly Powered by AbleSci AI