Ghodake Gajanan S, Kalme Satish D, Jadhav Jyoti P, Govindwar Sanjay P
Department of Biochemistry, Shivaji University, Kolhapur 416004, India.
Appl Biochem Biotechnol. 2009 Jan;152(1):6-14. doi: 10.1007/s12010-008-8258-4. Epub 2008 May 28.
Lignin peroxidase was purified (72-fold) from Acinetobacter calcoaceticus NCIM 2890. The purified lignin peroxidase (55-65 kDa) showed dimeric nature. The maximum enzyme activity was observed at pH 1.0, between a broad temperature range of 50 and 70 degrees C, at H2O2 concentration (40 mM) and the substrate concentration (n-propanol, 100 mM). Purified lignin peroxidase was able to oxidize a variety of substrates including Mn2+, tryptophan, mimosine, L-Dopa, hydroquinone, xylidine, n-propanol, veratryl alcohol, and ten textile dyes of various groups indicating as a versatile peroxidase. Most of the dyes decolorized up to 90%. Tryptophan stabilizes the lignin peroxidase activity during decolorization of dyes.
从醋酸钙不动杆菌NCIM 2890中纯化得到木质素过氧化物酶（纯化倍数为72倍）。纯化后的木质素过氧化物酶（55 - 65 kDa）呈现二聚体性质。在pH 1.0、50至70摄氏度的较宽温度范围内、H2O2浓度为40 mM以及底物浓度（正丙醇，100 mM）时观察到最大酶活性。纯化后的木质素过氧化物酶能够氧化多种底物，包括Mn2+、色氨酸、含羞草碱、L - 多巴、对苯二酚、二甲苯胺、正丙醇、藜芦醇以及十种不同类别的纺织染料，表明其为一种多功能过氧化物酶。大多数染料的脱色率高达90%。在染料脱色过程中，色氨酸可稳定木质素过氧化物酶的活性。
