ACTIVITY OF LIGNINASE PEROXIDASE FROM ACINETOBACTER-ANITRATUS AND THE DEGRADATION OF PINUS-PINASTER LIGNIN

被引：8

作者：

LOPRETTI, MI ^{[1
]}

MATHIAS, AL ^{[1
]}

RODRIGUES, AE ^{[1
]}

机构：

[1] UNIV PORTO, SCH ENGN, SEPARAT & REACT ENGN LAB, P-4099 OPORTO, PORTUGAL

来源：

PROCESS BIOCHEMISTRY | 1993年 / 28卷 / 08期

关键词：

D O I：

10.1016/0032-9592(93)85016-9

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：

The ligninase activity of Acinetobacter anitratus cells and enzyme extracted from that bacterium was measured with a model substrate (benzyl alcohol) and two lignin substrates. Pinus pinaster lignin precipitated from kraft black liquor and treated black liquor. The activity of this intracellular enzyme was confirmed on benzyl alcohol, showing a sigmoid Michaelis curve for constant H2O2 concentration. Enzymatic activity on treated black liquor leads to the production of low molecular weight compounds and to partial polymerisation of lignin. The evolution of the molecular weight distribution of the original sample with time was followed by high pressure liquid chromatography.

引用

页码：543 / 547

页数：5

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