Recombinant expression and purification of an Oxysterol Binding Protein from Aspergillus oryzae

被引：1
|
作者：
Zhang, Xian [1 ]
Liu, Lanlan [1 ]
Hu, Jianwen [1 ]
Chen, Fei [1 ]
Zeng, Bin [1 ]
机构：
[1] Jiangxi Sci & Technol Normal Univ, Sch Life Sci, Nanchang, Jiangxi, Peoples R China
来源：
2016 INTERNATIONAL CONFERENCE ON MEDICINE SCIENCES AND BIOENGINEERING (ICMSB2016) | 2017年 / 8卷
关键词：
OSBP-RELATED PROTEINS; FAMILY;
D O I：
10.1051/bioconf/20170803006
中图分类号：
Q [生物科学];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
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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页数：6
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