Recombinant expression and purification of an Oxysterol Binding Protein from Aspergillus oryzae 3.042
A full-length cDNA encoding a candidate Oxysterol-binding protein(OSBP) from Aspergillus oryzae (AoOSBP) was cloned and expressed in Escherichia coli as a maltose-binding protein (MBP) fusion protein. The MBP-AoOSBP protein from the importantly industrial fungus A. oryzae was purified by amylose res...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
EDP Sciences
2017-01-01
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| Series: | BIO Web of Conferences |
| Online Access: | http://dx.doi.org/10.1051/bioconf/20170803006 |
| Summary: | A full-length cDNA encoding a candidate Oxysterol-binding protein(OSBP) from Aspergillus oryzae (AoOSBP) was cloned and expressed in Escherichia coli as a maltose-binding protein (MBP) fusion protein. The MBP-AoOSBP protein from the importantly industrial fungus A. oryzae was purified by amylose resin and chromatography column. SDS-PAGE showed that MBP-AoOSBP has an estimated molecular weight of 182 kDa. OSBP and its homologues (ORPs) own the affinity for oxysterols, cholesterol and glycerophospholipids. According to the superiority of A. oryzae in the fermented foods and also in food-grade productions pharmaceutical enzyme manufacture, it is meaningful to identify the biochemical properties of OSBP in A. oryzae. |
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| ISSN: | 2117-4458 |