漆酶
化学
叠氮化钠
色谱法
双酚A
荧光假单胞菌
核化学
酶
有机化学
细菌
遗传学
生物
环氧树脂
作者
Amar A. Telke,Dayanand Kalyani,Umesh Jadhav,Ganesh K. Parshetti,Sanjay P. Govindwar
出处
期刊:Journal of Molecular Catalysis B-enzymatic
[Elsevier]
日期:2009-12-01
卷期号:61 (3-4): 252-260
被引量:83
标识
DOI:10.1016/j.molcatb.2009.08.001
摘要
The Pseudomonas sp. LBC1 produced extracellular laccase when grown in the nutrient broth. The enzyme was purified using acetone precipitation and an anion-exchange chromatography. The molecular weight of the purified laccase was estimated as 70 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. An enzyme showed maximum substrate specificity towards o-tolidine than other substrates of laccase including 2,2′-azinobis, 3-ethylbenzothiazoline-6-sulfonic acid, hydroquinone, N,N′-dimethyl phenylene diamine, syringic acid and veratryl alcohol. The optimum pH and temperature for the laccase activity were 4.0 and 40 °C, respectively. Cyclic voltammogram revealed the redox potential of purified enzyme as 0.30 V. The laccase was stable up to 40 °C and within pH range 6.0–8.0. Sodium azide and EDTA strongly inhibited laccase activity. The purified laccase completely degraded the higher concentration of bisphenol A within 5 h. Biodegradation metabolites of bisphenol A were characterized by using FTIR, HPLC and GC–MS.
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