Expression and biochemical characterization of recombinant α-l-rhamnosidase r-Rha1 from Aspergillus niger JMU-TS528
详细信息 查看全文
- 作者：Lijun Lia ; b ; c ; Yue Yua ; Xia Zhanga ; Zedong Jianga ; b ; c ; Yanbing Zhua ; b ; c ; Anfeng Xiaoa ; b ; c ; Hui Nia ; b ; c ; nihui@jmu.edu.cn" class="auth_mail" title="E-mail the corresponding author ; Feng Chena ; d
- 关键词：PCR ; polymerase chain reaction ; cDNA ; complementary deoxyribonucleic acid ; RT-PCR ; reverse transcription-polymerase chain reaction ; BMGY ; buffered glycerol-complex medium ; BMMY ; buffered methanol-complex medium ; YNB ; yeast nitrogen base ; SDS ; sodium dodecyl sulphate ; PAGE ; polyacrylamide gel electrophoresis ; CBB ; coomassie brilliant blue ; MALDI-TOF ; matrix-assisted laser desorption/ionization time of flight ; MS ; mass spectrometry ; HPLC ; high performance liquid chromatography ; pNPR ; 4-nitrophenyl
- 刊名：International Journal of Biological Macromolecules
- 出版年：2016
- 出版时间：April 2016
- 年：2016
- 卷：85
- 期：Complete
- 页码：391-399
- 全文大小：933 K
文摘
- •
We cloned a putative cDNA of α--rhamnosidase from Aspergillus niger JMU-TS528 and extracellular over-expressed this cDNA in Pichia pastoris GS115.
- •
The activity of the recombinant α--rhamnosidase r-Rha1 is eightfold higher than the native enzyme.
- •
r-Rha1 is a N-glycosylated protein possessed broad substrate specificities, a good thermostability, wide range of pH-stability, and excellent tolerance abilities against glucose and ethanol.