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| Teh,Ser Huy; Fong,Mun Yik; Mohamed,Zulqarnain. |
| The Pichia pastoris expression system was used to produce recombinant human erythropoietin, a protein synthesized by the adult kidney and responsible for the regulation of red blood cell production. The entire recombinant human erythropoietin (rhEPO) gene was constructed using the Splicing by Overlap Extension by PCR (SOE-PCR) technique, cloned and expressed through the secretory pathway of the Pichia expression system. Recombinant erythropoietin was successfully expressed in P. pastoris. The estimated molecular mass of the expressed protein ranged from 32 kDa to 75 kDa, with the variation in size being attributed to the presence of rhEPO glycosylation analogs. A crude functional analysis of the soluble proteins showed that all of the forms were active in... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Erythropoietin; Glycosylation; Pichia pastoris; SOE-PCR. |
| Ano: 2011 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572011000300017 |
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| Ahmed,Samia A.; El-Shayeb,Nefisa M.A.; Hashem,Abdel-Gawad M.; Saleh,Shireen A.A.; Abdel-Fattah,Ahmed F.. |
| Aspergillus niger β-glucosidase was modified by covalent coupling to periodate activated polysaccharides (glycosylation). The conjugated enzyme to activated starch showed the highest specific activity (128.5 U/mg protein). Compared to the native enzyme, the conjugated form exhibited: a higher optimal reaction temperature, a lower Ea (activation energy), a higher Km (Michaelis constant) and Vmax (maximal reaction rate), and improved thermal stability. The calculated t1/2 (half-life) values of heat in-activation at 60 °C and 70 °C were 245.7 and 54.5 min respectively, whereas at these temperatures the native enzyme was less stable (t1/2of 200.0 and 49.5 min respectively). The conjugated enzyme retained 32.3 and 29.7%, respectively from its initial activity... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Β-glucosidases; Glycosylation; Soluble polysaccharides; Enzyme stability. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822015000100023 |
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