AN IMPROVED METHOD FOR THE PURIFICATION OF LIGNIN PEROXIDASES FROM PHANEROCHAETE-CHRYSOSPORIUM INA-12 - PROPERTIES OF 2 MAJOR ISOFORMS

被引：9

作者：

ASTHER, M ^{[1
]}

VILTER, H ^{[1
]}

KUREK, B ^{[1
]}

MEUNIER, JC ^{[1
]}

机构：

[1] INST NATL AGRON PARIS GRIGNON, CTR BIOTECHNOL AGROIND, CHIM BIOL LAB, F-78850 THIVERVAL GRIGNON, FRANCE

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY | 1992年 / 24卷 / 09期

关键词：

D O I：

10.1016/0020-711X(92)90062-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

1. Phanerochaete chrysosporium INA-12 secretes several lignin peroxidase isoenzymes. This paper reports an improved procedure for the purification of the different isoforms compared to those previously described. 2. Lignin peroxidases are first concentrated and prefractionated on fast-flow ion-exchangers which avoid concentration by ultrafiltration and dialysis. 3. Further purification is achieved by hydrophobic interaction chromatography and anion-exchange FPLC. 4. Two major forms were purified to homogeneity. Kinetic measurements and protein characterization (isoelectric points, phosphate content) suggest that they are similar to those produced by P. chrysosporium BKM strain.

引用

页码：1377 / 1383

页数：7

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