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Details for article 73 of 129 found articles
| Title: |
Glycosylation and pH stability of penicillin G acylase from providencia rettgeri produced in Pichia pastoris |
| Author: |
Šenerović Lidija Stanković Nad Ljubijankić G. Vasiljević Branka |
| Appeared in: |
Archives of biological sciences |
| Paging: | Volume 61 (2009) nr. 4 pages 581-586 |
| Year: |
2009 |
| Contents: |
Penicillin G acylase (PAC) is one of the most widely used enzymes in industrial synthesis of semi-synthetic antibiotics. The Providencia rettgeri pac gene was expressed to a level of 2.7 U/ml using the Pichia pastoris expression system. The recombinant enzyme was purified and its glycosylation status was determined. It was found that both subunits (α and β) of the enzyme were N-glycosylated, while the β-subunit also contained O-glycans. It was also observed that rPACP.rett. was stable in a wide range of pH, which, in addition to the previously proved high thermostability, makes it an attractive biocatalyst from an industrial point of view. |
| Publisher: |
Srpsko biološko društvo, Institut za biološka istraživanja "Siniša Stanković", Biološki fakultet Univerziteta u Beogradu, Institut za primenu nuklearne energije u poljoprivredi, šumarstvu i veterinarstvu (provided by DOAJ) |
| Source file: |
Elektronische Wetenschappelijke Tijdschriften |
Details for article 73 of 129 found articles
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