Koroleva O V, Yavmetdinov I S, Shleev S V, Stepanova E V, Gavrilova V P
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 117071, Russia.
Biochemistry (Mosc). 2001 Jun;66(6):618-22. doi: 10.1023/a:1010299012591.
A new strain producing extracellular laccase (Cerrena maxima 0275) was found by screening of isolates of Basidiomycetes, and the dynamics of laccase biosynthesis by this strain was studied. The enzyme was purified to homogeneity. The molecular weight of the enzyme is 57 kD, and its pI is 3.5. The activity is constant at pH values in the range 3.0-5.0. The temperature optimum for activity is 50 degrees C. The thermal stability of the laccase was studied. The catalytic and Michaelis constants for catechol, hydroquinone, sinapinic acid, and K4Fe(CN)6 were determined. The standard redox potential of type 1 copper in the enzyme is 750 +/- 5 mV. Thus, the investigated laccase is a high redox potential laccase.
通过筛选担子菌分离物,发现了一种能产生胞外漆酶的新菌株(大孢蜡蘑0275),并研究了该菌株漆酶生物合成的动力学。该酶被纯化至同质。酶的分子量为57 kD,其等电点为3.5。在pH值3.0 - 5.0范围内活性恒定。活性的最适温度为50℃。研究了漆酶的热稳定性。测定了儿茶酚、对苯二酚、芥子酸和K4Fe(CN)6的催化常数和米氏常数。该酶中1型铜的标准氧化还原电位为750±5 mV。因此,所研究的漆酶是一种高氧化还原电位漆酶。