THERMOSTABLE EXTRACELLULAR PEROXIDASES FROM STREPTOMYCES-THERMOVIOLACEUS

被引:26
作者
IQBAL, M [1 ]
MERCER, DK [1 ]
MILLER, PGG [1 ]
MCCARTHY, AJ [1 ]
机构
[1] UNIV LIVERPOOL, DEPT GENET & MICROBIOL, LIVERPOOL L69 3BX, ENGLAND
来源
MICROBIOLOGY-SGM | 1994年 / 140卷
关键词
STREPTOMYCES THERMOVIOLACEUS; EXTRACELLULAR PEROXIDASES; THERMOSTABILITY;
D O I
10.1099/00221287-140-6-1457
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Streptomyces thermoviolaceus is a thermophilic actinomycete that was found to produce relatively large amounts of extracellular peroxidase activity when grown on xylan as primary carbon source. The activity was due to multiple isoforms of peroxidase, of which two, designated P-3 and P-5, were predominant. The two proteins were purified to homogeneity by a combination of ultrafiltration, ammonium sulphate precipitation, anion-exchange chromatography, gel filtration and preparative gel electrophoresis. The peroxidases were found to be haemoproteins that catalysed the oxidation of a range of substrates in the presence of hydrogen peroxide. Both are monomeric acidic proteins (P-3: 82 kDa, pl 5.0; P-5: 60 kDa, pl 4.75) but with some differences in substrate specificity, P-3 exhibiting the broader substrate range. Peroxidase activity was optimal at ph values close to neutrality, and both enzymes were robust, exhibiting activity at elevated temperatures in the presence of denaturing agents such as SDS or 8 M urea. Peroxidase P-3 was stable at 50 degrees C for more than 24 h and had a half-life of 70 min at 70 degrees C. Polyclonal antibodies prepared against each isoform cross-reacted, indicating that the proteins were antigenically related. No cross-reactions were detected against horseradish peroxidase or crude peroxidase preparations from two other thermophilic streptomycetes.
引用
收藏
页码:1457 / 1465
页数:9
相关论文
共 34 条
  • [1] PRODUCTION OF MAJOR EXTRACELLULAR ENZYMES DURING LIGNOCELLULOSE DEGRADATION BY 2 STREPTOMYCETES IN AGITATED SUBMERGED CULTURE
    ADHI, TP
    KORUS, RA
    CRAWFORD, DL
    [J]. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1989, 55 (05) : 1165 - 1168
  • [2] LIGNOCARBOHYDRATE SOLUBILIZATION FROM STRAW BY ACTINOMYCETES
    BALL, AS
    GODDEN, B
    HELVENSTEIN, P
    PENNINCKX, MJ
    MCCARTHY, AJ
    [J]. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1990, 56 (10) : 3017 - 3022
  • [3] BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
  • [4] IDENTIFICATION OF A SPECIFIC MANGANESE PEROXIDASE AMONG LIGNINOLYTIC ENZYMES SECRETED BY PHANEROCHAETE-CHRYSOSPORIUM DURING WOOD DECAY
    DATTA, A
    BETTERMANN, A
    KIRK, TK
    [J]. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1991, 57 (05) : 1453 - 1460
  • [5] Everse, 1990, PEROXIDASES CHEM BIO, V1
  • [6] PHYSICAL AND ENZYMATIC-PROPERTIES OF LIGNIN PEROXIDASE ISOENZYMES FROM PHANEROCHAETE-CHRYSOSPORIUM
    FARRELL, RL
    MURTAGH, KE
    TIEN, M
    MOZUCH, MD
    KIRK, TK
    [J]. ENZYME AND MICROBIAL TECHNOLOGY, 1989, 11 (06) : 322 - 329
  • [7] LIGNIN PEROXIDASE FROM CHRYSONILIA-SITOPHILA - HEAT-DENATURATION KINETICS AND PH STABILITY
    FERRER, I
    ESPOSITO, E
    DURAN, N
    [J]. ENZYME AND MICROBIAL TECHNOLOGY, 1992, 14 (05) : 402 - 406
  • [8] TOWARDS ELUCIDATION OF THE LIGNIN DEGRADATION PATHWAY IN ACTINOMYCETES
    GODDEN, B
    BALL, AS
    HELVENSTEIN, P
    MCCARTHY, AJ
    PENNINCKX, MJ
    [J]. JOURNAL OF GENERAL MICROBIOLOGY, 1992, 138 : 2441 - 2448
  • [9] GOLD MH, 1989, ACS SYM SER, V389, P127
  • [10] GOLD MH, 1993, PLANT PEROXIDASES BI, P87