Back to Search
Start Over
High level expression and characterization of tannase tan7 using Aspergillus niger SH-2 with low-background endogenous secretory proteins as the host
- Source :
- Protein expression and purification. 144
- Publication Year :
- 2017
-
Abstract
- Tannin acyl hydrolase (tannase, EC3.1.1.20) catalyzes the hydrolysis of hydrolyzable tannins. It is used in the manufacture of instant tea and in the production of gallic acid. In this study, we reported that the overexpression, purification and characterization of an Aspergillus niger tannase. The tannase gene was cloned from A. niger SH-2 and expressed in the A. niger strain Bdel4 which is low-background of secreted proteins. The recombinant tannase was purified by desalting, followed by gel filtration for characterization. The tannase activity achieved 111.5 U/mL at 168 h, and the purity of the enzyme in the broth supernatant was estimated to be over 70%. The optimum temperature and pH of the recombinant tannase was ∼40 °C and 7.0, respectively. The tannase activity was inhibited by Mg2+, Ca2+, Cu2+, Ba2+, Ni2+ and EDTA, and was enhanced by Mn2+ and Co2+. Since A. niger is a GRAS microorganism, the recombinant tannase could be purification-free due to its high purity. The results of this study suggested that this recombinant strain could be subjected to large-scale production of A. niger tannase.
- Subjects :
- 0106 biological sciences
0301 basic medicine
Tannase activity
01 natural sciences
Tannase
law.invention
Fungal Proteins
03 medical and health sciences
Hydrolysis
chemistry.chemical_compound
law
010608 biotechnology
Hydrolase
Tannin
Gallic acid
Cloning, Molecular
chemistry.chemical_classification
biology
fungi
Aspergillus niger
biology.organism_classification
Recombinant Proteins
030104 developmental biology
chemistry
Biochemistry
Recombinant DNA
Carboxylic Ester Hydrolases
Biotechnology
Subjects
Details
- ISSN :
- 10960279
- Volume :
- 144
- Database :
- OpenAIRE
- Journal :
- Protein expression and purification
- Accession number :
- edsair.doi.dedup.....f97f83e9791763a8b4dc561cb69e7283