PHYTASE FROM BACILLUS SP. STRAIN LA12: ISOLATION, PURIFICATION AND CHARACTERIZATION

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Udgivet i:The Journal of Microbiology, Biotechnology and Food Sciences vol. 10, no. 4 (Feb/Mar 2021), p. 572
Hovedforfatter: Abdolshahi, Anna
Andre forfattere: Behdad Shokrollahi Yancheshmeh, Arabameri, Majid, Marvdashti, Leila Monjazeb
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Faculty of Biotechnology and Food Sciences
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022 |a 1338-5178 
024 7 |a 10.15414/jmbfs.2021.10.4.572-576  |2 doi 
035 |a 2575863092 
045 2 |b d20210201  |b d20210331 
084 |a 187029  |2 nlm 
100 1 |a Abdolshahi, Anna 
245 1 |a PHYTASE FROM BACILLUS SP. STRAIN LA12: ISOLATION, PURIFICATION AND CHARACTERIZATION 
260 |b Faculty of Biotechnology and Food Sciences  |c Feb/Mar 2021 
513 |a Journal Article 
520 3 |a Phytate take effect as an anti-nutrient element in food and feed materials. Thus, phytase, by catalyzing phytate, hydrolyzing the phosphomonoester bonds and releasing the inorganic phosphorous, decrease the phytate and enhance their nutritional value. Therefore, in this study, Bacillus sp. strain LA12was isolated from natural origins and the phytase production activity was evaluated. The novel extracellular phytase was produced and precipitated by saturated ammonium sulfate. The ion-exchange chromatography on DEAE-sepharose and the size-exclusion chromatography on Sephadex G-100 were used to purify the enzyme. The results showed that the purification yield and concentration of final enzyme were 5.9% and 18.4%, respectively. Based on SDS-PAGE results the molecular weight of the phytase was determined about 73 kDa. Optimal activity of the enzyme was obtained at pH of 5.5 and 60 ºC. Kinetic parameters Km and Vmax were 0.197 mM and 1.174 µmol/min, respectively. Mg2+, Co2+ and EDTA accelerated the effect on phytase activity; whilst adding other metal ions such as Ca2+, Zn2+ and Fe2+ in both concentrations could decrease its activity. Moreover, ‏ Mn2+ ion didn’t show indicative effect on its activity. The purified phytase exhibits good thermal stability after incubation at 50-70°C for 30 min, whereas the phytase activity drastically decreased up to 61% at 80°C. This study indicated that the purified phytase has the desired characteristics and can promisingly be used for hydrolyzing of phytate in food and feed. 
653 |a Gel electrophoresis 
653 |a Phytase 
653 |a Thermal stability 
653 |a Ammonium 
653 |a Calcium 
653 |a Ammonium sulfate 
653 |a Zinc 
653 |a Cobalt 
653 |a Nutritive value 
653 |a Chromatography 
653 |a Magnesium 
653 |a Food 
653 |a Purification 
653 |a Iron 
653 |a Carbon dioxide 
653 |a Manganese ions 
653 |a Ethylenediaminetetraacetic acids 
653 |a Sodium lauryl sulfate 
653 |a Metal ions 
653 |a Molecular weight 
653 |a Enzymes 
653 |a Ion-exchange chromatography 
653 |a Calcium ions 
653 |a Size exclusion chromatography 
653 |a Ion exchange 
653 |a Environmental 
700 1 |a Behdad Shokrollahi Yancheshmeh 
700 1 |a Arabameri, Majid 
700 1 |a Marvdashti, Leila Monjazeb 
773 0 |t The Journal of Microbiology, Biotechnology and Food Sciences  |g vol. 10, no. 4 (Feb/Mar 2021), p. 572 
786 0 |d ProQuest  |t Agriculture Science Database 
856 4 1 |3 Citation/Abstract  |u https://www.proquest.com/docview/2575863092/abstract/embedded/7BTGNMKEMPT1V9Z2?source=fedsrch 
856 4 0 |3 Full Text - PDF  |u https://www.proquest.com/docview/2575863092/fulltextPDF/embedded/7BTGNMKEMPT1V9Z2?source=fedsrch