Screening of phytase producers and optimization of culture conditions for submerged fermentation

Hasan B. Coban, Ali Demirci

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)609-616
Number of pages8
JournalBioprocess and biosystems engineering
Volume37
Issue number4
DOIs
StatePublished - Jan 1 2014

Fingerprint

6-Phytase
Fermentation
Screening
Microorganisms
Orthophosphoric acid
Phytic Acid
Aspergillus
Medical applications
Enzymes
Temperature
Inositol
Phosphoric Monoester Hydrolases

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering

Cite this

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Screening of phytase producers and optimization of culture conditions for submerged fermentation. / Coban, Hasan B.; Demirci, Ali.

In: Bioprocess and biosystems engineering, Vol. 37, No. 4, 01.01.2014, p. 609-616.

Research output: Contribution to journalArticle

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AU - Demirci, Ali

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