ISOLATION, CHARACTERIZATION AND FUNCTION OF IACCASE FROM TRICHODERMA

被引:50
作者
ASSAVANIG, A [1 ]
AMORNKITTICHAROEN, B [1 ]
EKPAISAL, N [1 ]
MEEVOOTISOM, V [1 ]
FLEGEL, TW [1 ]
机构
[1] MAHIDOL UNIV,FAC SCI,DEPT MICROBIOL,BANGKOK 10700,THAILAND
关键词
D O I
10.1007/BF00174468
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Of fourteen natural isolates of Trichoderma, no correlation was found between substrate weight loss and phenol oxidase (PO) activity in rice straw cultures. The highest PO producer from these laccase-positive strains was subjected to UV mutagenesis in order to select high and low PO activity mutants. There was no significant difference in substrate weight loss for mutant strains with six times higher and six times lower PO activity than the parent strain. Nor did the enzyme activity result in decreased growth inhibition by inhibitory phenolic compounds. PO enzyme from the parent Trichoderma and one of its high-PO-activity mutants was subsequently purified by ethanol precipitation from liquid cultures optimized by supplementation with copper sulphate and cycloheximide. Protein staining and activity staining of disc electrophoresis gels showed that only one PO enzyme of approximately 71 000 Da was produced. The enzyme could be defined as a laccase (benzenediol: oxygen oxidoreductase E.C. 1.10.3.2) because it catalysed the oxidation of syringaldazine and p-phenylenediamine in the absence of hydrogen peroxide, and because it was inhibited by cetyltrimethylammonium bromide but not by cinnamic acid. No specific in-vivo function could be assigned to this enzyme.
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页码:198 / 202
页数:5
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