Screening of phytase producers and optimization of culture conditions for submerged fermentation
Phytase (myo-inositol-hexakisphosphate phosphohydrolase) is an enzyme, which breaks down phytate to inositol and orthophosphoric acid. Phytase has been used as feed additive, and in some medical applications for years. To date, phytase production has been usually performed as a solid-state fermentat...
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Published in | Bioprocess and biosystems engineering Vol. 37; no. 4; pp. 609 - 616 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Berlin/Heidelberg
Springer Berlin Heidelberg
01.04.2014
Springer Nature B.V |
Subjects | |
Online Access | Get full text |
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Summary: | Phytase (myo-inositol-hexakisphosphate phosphohydrolase) is an enzyme, which breaks down phytate to inositol and orthophosphoric acid. Phytase has been used as feed additive, and in some medical applications for years. To date, phytase production has been usually performed as a solid-state fermentation with small production volumes. Therefore, the aim of this study was to increase the phytase activity in submerged fermentations by screening several microorganism strains based on the literature to select the most productive phytase producer and optimizing growth parameters such as temperature, pH, and aeration level using response surface methodology (RSM). As a result, among the four different microorganisms evaluated,
Aspergillus ficuum
(NRRL 3135) was selected as the most productive strain. Optimum temperature, pH, and aeration values were determined as 33 °C, 4.5, and 0.9 vvm, respectively, for
A. ficuum
in 2-l batch submerged phytase productions. Under these conditions, phytase activity was measured as 2.27 U/ml. Therefore, this is a unique study showing the production of phytase with
A. ficuum
successfully in submerged fermentation as opposed to the traditional solid-state fermentation. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1615-7591 1615-7605 |
DOI: | 10.1007/s00449-013-1028-x |