Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan:: reconstitution of the in vivo system from recombinant enzymes

被引:74
作者
Adelsberger, H
Hertel, C
Glawischnig, E
Zverlov, VV
Schwarz, WH
机构
[1] Tech Univ Munich, Res Grp Microbial Biotechnol, D-85350 Freising Weihenstephan, Germany
[2] Russian Acad Sci, Inst Mol Genet, Moscow 123182, Russia
来源
MICROBIOLOGY-SGM | 2004年 / 150卷
关键词
D O I
10.1099/mic.0.27066-0
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Four extracellular enzymes of the thermophilic bacterium Clostridium stercorarium are involved in the depolymerization of de-esterified arabinoxylan: Xyn11A, Xyn10C, Bxl3B, and Arf51B. They were identified in a collection of eight clones producing enzymes hydrolysing xylan (xynA, xynB, xynC), beta-xyloside (bxlA, bxlB, bglZ) and alpha-arabinofuranoside (arfA, arfB). The modular enzymes Xyn11A and Xyn10C represent the major xylanases in the culture supernatant of C. stercorarium. Both hydrolyse arabinoxylan in an endo-type mode, but differ in the pattern of the oligosaccharides produced. Of the glycosidases, Bxl3B degrades xylobiose and xylooligosaccharides to xylose, and Arf51B is able to release arabinose residues from de-esterified arabinoxylan and from the oligosaccharides generated. The other glycosidases either did not attack or only marginally attacked these oligosaccharides. Significantly more xylanase and xylosidase activity was produced during growth on xylose and xylan. This is believed to be the first time that, in a single thermophilic micro-organism, the complete set of enzymes (as well as the respective genes) to completely hydrolyse de-esterified arabinoxylan to its monomeric sugar constituents, xylose and arabinose, has been identified and the enzymes produced in vivo. The active enzyme system was reconstituted in vitro from recombinant enzymes.
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页码:2257 / 2266
页数:10
相关论文
共 44 条
[1]  
Ali MK, 2001, FEMS MICROBIOL LETT, V198, P79
[2]   Cloning, sequencing, and expression of the gene encoding the Clostridium stercorarium xylanase C in Escherichia coli [J].
Ali, MK ;
Fukumura, M ;
Sakano, K ;
Karita, S ;
Kimura, T ;
Sakka, K ;
Ohmiya, K .
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 1999, 63 (09) :1596-1604
[3]  
[Anonymous], [No title captured]
[4]   Microbial xylanases and their industrial applications: a review [J].
Beg, QK ;
Kapoor, M ;
Mahajan, L ;
Hoondal, GS .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2001, 56 (3-4) :326-338
[5]   PRODUCTION, PURIFICATION, AND PROPERTIES OF THERMOSTABLE XYLANASE FROM CLOSTRIDIUM-STERCORARIUM [J].
BERENGER, JF ;
FRIXON, C ;
BIGLIARDI, J ;
CREUZET, N .
CANADIAN JOURNAL OF MICROBIOLOGY, 1985, 31 (07) :635-643
[6]   SEPARATION OF THE CELLULOLYTIC AND XYLANOLYTIC ENZYMES OF CLOSTRIDIUM-STERCORARIUM [J].
BRONNENMEIER, K ;
EBENBICHLER, C ;
STAUDENBAUER, WL .
JOURNAL OF CHROMATOGRAPHY, 1990, 521 (02) :301-310
[7]   ALPHA-D-GLUCURANIDASES FROM THE XYLANOLYTIC THERMOPHILES CLOSTRIDIUM-STERCORARIUM AND THERMOANAEROBACTERIUM-SACCHAROLYTICUM [J].
BRONNENMEIER, K ;
MEISSNER, H ;
STOCKER, S ;
STAUDENBAUER, WL .
MICROBIOLOGY-SGM, 1995, 141 :2033-2040
[8]  
Bronnenmeier K, 1996, BIOSEPARATION, V6, P41
[9]  
Coutinho PM, 1999, ROY SOC CH, P3
[10]  
COUTINHO PM, 1999, GENETICS BIOCH ECOLO, P15