Chitinolytic enzymes from Clostridium aminovalericum: activity screening and purification
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
15227797
DOI
10.1007/bf02931401
Knihovny.cz E-resources
- MeSH
- Acetylglucosaminidase chemistry isolation & purification metabolism MeSH
- Amidohydrolases chemistry isolation & purification metabolism MeSH
- Chitin metabolism MeSH
- Chitinases chemistry isolation & purification metabolism MeSH
- Chromatography, Ion Exchange MeSH
- Clostridium enzymology isolation & purification metabolism MeSH
- Enzyme Induction MeSH
- Feces microbiology MeSH
- Glycoside Hydrolases chemistry isolation & purification metabolism MeSH
- Isoenzymes chemistry isolation & purification metabolism MeSH
- Goats microbiology MeSH
- Substrate Specificity MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Acetylglucosaminidase MeSH
- Amidohydrolases MeSH
- chitin deacetylase MeSH Browser
- Chitin MeSH
- Chitinases MeSH
- chitosanase MeSH Browser
- Glycoside Hydrolases MeSH
- Isoenzymes 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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