Production of feed enzymes (phytase and plant cell wall hydrolyzing enzymes) by Mucor indicus MTCC 6333: purification and characterization of phytase
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
18298046
DOI
10.1007/bf02932109
Knihovny.cz E-resources
- MeSH
- 6-Phytase chemistry isolation & purification metabolism MeSH
- alpha-Amylases metabolism MeSH
- Cell Wall metabolism MeSH
- Cellulase metabolism MeSH
- Endo-1,4-beta Xylanases metabolism MeSH
- Fermentation MeSH
- Chromatography, Gel MeSH
- Hydrolases metabolism MeSH
- Hydrogen-Ion Concentration MeSH
- Animal Feed MeSH
- Culture Media chemistry MeSH
- Mucor enzymology growth & development isolation & purification MeSH
- Dietary Fiber microbiology MeSH
- Industrial Microbiology * MeSH
- Enzyme Stability MeSH
- Substrate Specificity MeSH
- Temperature MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- 6-Phytase MeSH
- alpha-Amylases MeSH
- carboxymethylcellulase MeSH Browser
- Cellulase MeSH
- Endo-1,4-beta Xylanases MeSH
- Hydrolases MeSH
- Culture Media MeSH
- Dietary Fiber MeSH
The production of phytase and associated feed enzymes (phosphatase, xylanase, CMCase, alpha-amylase and beta-glucosidase) was determined in a thermotolerant fungus Mucor indicus MTCC 6333, isolated from composting soil. Solid-substrate culturing on wheat bran and optimizing other culture conditions (C and N sources, level of N, temperature, pH, culture age, inoculum level), increased the yield of phytase from 266 +/- 0.2 to 513 +/- 0.4 nkat/g substrate dry mass. The culture extract also contained 112, 194, 171, 396, and 333 nkat/g substrate of phosphatase, xylanase, CMCase, beta-glucosidase and alpha-amylase activities, respectively. Simple 2-step purification employing anion exchange and gel filtration chromatography resulted in 21.9-fold purified phytase. The optimum pH and temperature were pH 6.0 and 70 degrees C, respectively. The phytase was thermostable under acidic conditions, showing 82% residual activity after exposure to 60 degrees C at pH 3.0 and 5.0 for 2 h, and displayed broad substrate specificity. The Km was 200 nmol/L and v(lim) of 113 nmol/s per mg protein with dodecasodium phytate as substrate. In vitro feed trial with feed enzyme resulted in the release of 1.68 g inorganic P/kg of feed after 6 h of incubation at 37 degrees C.
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