Chitinolytic enzymes from Clostridium aminovalericum: activity screening and purification
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
15227797
DOI
10.1007/bf02931401
Knihovny.cz E-zdroje
- MeSH
- acetylglukosaminidasa chemie izolace a purifikace metabolismus MeSH
- amidohydrolasy chemie izolace a purifikace metabolismus MeSH
- chitin metabolismus MeSH
- chitinasy chemie izolace a purifikace metabolismus MeSH
- chromatografie iontoměničová MeSH
- Clostridium enzymologie izolace a purifikace metabolismus MeSH
- enzymová indukce MeSH
- feces mikrobiologie MeSH
- glykosidhydrolasy chemie izolace a purifikace metabolismus MeSH
- izoenzymy chemie izolace a purifikace metabolismus MeSH
- kozy mikrobiologie MeSH
- substrátová specifita MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- acetylglukosaminidasa MeSH
- amidohydrolasy MeSH
- chitin deacetylase MeSH Prohlížeč
- chitin MeSH
- chitinasy MeSH
- chitosanase MeSH Prohlížeč
- glykosidhydrolasy MeSH
- izoenzymy MeSH
A strain isolated from the feces of takin was identified as Clostridium aminovalericum. In response to various types of chitin used as growth substrates, the bacterium produced a complete array of chitinolytic enzymes: chitinase ('endochitinase'), exochitinase, beta-N-acetylglucosaminidase, chitosanase and chitin deacetylase. The highest activities of chitinase (536 pkat/mL) and exochitinase (747 pkat/mL) were induced by colloidal chitin. Fungal chitin also induced high levels of these enzymes (463 pkat/mL and 502 pkat/mL, respectively). Crab shell chitin was the best inducer of chitosanase activity (232 pkat/mL). The chitinolytic enzymes of this strain were separated from culture filtrate by ion-exchange chromatography on the carboxylic sorbent Polygran 27. At pH 4.5, some isoforms of the chitinolytic enzymes (30% of total enzyme activity) did not bind to Polygran 27. The enzymes were eluted under a stepwise pH gradient (pH 5-8) in 0.1 mol/L phosphate buffer. At merely acidic pH (4.5-5.5), the adsorbed enzymes were co-eluted. However, at pH close to neutral values, the peaks of highly purified isoforms of exochitinases and chitinases were isolated. The protein and enzyme recovery reached 90%.
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Appl Environ Microbiol. 1995 May;61(5):1720-6 PubMed
Vopr Med Khim. 1978 Jul-Aug;24(4):569-72 PubMed
Biosci Biotechnol Biochem. 1996 Oct;60(10):1598-603 PubMed
Can J Microbiol. 1993 Jan;39(1):40-5 PubMed
Appl Environ Microbiol. 1998 Mar;64(3):890-5 PubMed
Folia Microbiol (Praha). 2001;46(1):76-8 PubMed
Anal Biochem. 1977 Jul;81(1):21-7 PubMed
Folia Microbiol (Praha). 2000;45(5):465-8 PubMed
J Bacteriol. 1997 Dec;179(23 ):7306-14 PubMed
Folia Microbiol (Praha). 2002;47(5):559-64 PubMed
Lett Appl Microbiol. 1997 Oct;25(4):284-8 PubMed
Appl Environ Microbiol. 1991 Feb;57(2):510-6 PubMed
Lett Appl Microbiol. 1996 Sep;23(3):195-8 PubMed
Anal Biochem. 1976 May 7;72:248-54 PubMed
Arch Microbiol. 2003 Dec;180(6):434-43 PubMed
Excretome of the chitinolytic bacterium Clostridium paraputrificum J4
Effect of gluten-free diet on microbes in the colon
Effect of chitosan on the growth of human colonic bacteria
