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Comparison of biochemical properties of recombinant phytase expression in the favorable methylotrophic platforms of Pichia pastoris and Hansenula polymorpha | ||
| Progress in Biological Sciences | ||
| مقاله 8، دوره 4، شماره 1، مرداد 2014، صفحه 97-111 اصل مقاله (644.98 K) | ||
| نوع مقاله: Original Research Papers | ||
| شناسه دیجیتال (DOI): 10.22059/pbs.2014.50309 | ||
| نویسندگان | ||
| Ardeshir Hesampour1؛ Omid Ranaei* 2؛ Mohammad Ali Malboobi1؛ Javad Harati3؛ Nooshin Mohandesi4 | ||
| 1Department of Plant Biotechnology, National Institute of Genetic Engineering and Biotechnology,,Tehran,IRAN(NIGEB) | ||
| 2Nanobiotechnology Engineering Laboratory , Shahid Beheshti University, ,Faculty of Energy and New Technologies,Tehran,IRAN | ||
| 3Nanobiotechnology Engineering Laboratory,Faculty of Energy and New Technologies,Shahid Beheshti University, ,Tehran,IRAN | ||
| 4Nanobiotechnology Engineering Laboratory ,Faculty of Energy and New Technologies,Shahid Beheshti University,Tehran,IRAN | ||
| چکیده | ||
| Phytic acid is the dominant form of phosphorous in plant seeds. However, phytic acid cannot be utilized by animals and causes them serious phosphate deficiency. Utilization of phytase as an animal feed additive can affect liberation of phosphor and its mineral availability. In this study, heterologous expression of the A. niger phyA gene was investigated in the methylotrophic yeasts P. pastoris and H.polymorpha and its expressed active recombinant phytase biochemical and biophysical properties were studies and compared to native A.niger phytase. The phyA gene sequence of A.niger was designed and expression of synthetic genes was highly successfully in active form in both yeast hosts. Size of the secreted recombinant phytases, due to heavy glycosylation, varied from 50 to 65 KDa. Expressed extracellular recombinant phytase samples were purified and biochemical tests on properties demonstrated that both recombinant phytase samples had similar pH profiles with pH optima determinations of pH 2.5, pH.5.5 as acid phosphatase and optimum temperature of 60 and 50 °C respectively in P. pastoris and H. polymorpha. This study concludes that recombinant P. pastoris and H. polymorpha phytases could fulfil a series of predefined industrial quality criteria for application as animal feed supplement. | ||
| کلیدواژه‌ها | ||
| Phytase؛ Pichia pastoris؛ Hansenula polymorpha | ||
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