http://rdf.ncbi.nlm.nih.gov/pubchem/patent/TN-2015000206-A1
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_f74b35f857361983324854bc89d9b1a4 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-52 |
| filingDate | 2015-05-25-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_6eb63b5f68168b378db3ab254ed8ce8f http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_7a3baa01b3f8af8ca456bb0ded9838eb http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_5bb24ff3835a213d4074a5c489ff8c29 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_bae6734da852bcf020f5adee60c0baeb http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_89672a82c6eb6a0910324e8aaf3db05b http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_c15d36b28b168da69b70e70e8626306d |
| publicationDate | 2016-10-03-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | TN-2015000206-A1 |
| titleOfInvention | Study of a new thermoactive and thermostable alkaline thiol-dependent serine protease serine produced by the strain of Streptomyces koyangensis TN650 having an industrial interest in peptide synthesis and in the formulation of washing detergents. |
| abstract | The present invention relates to the homogenous purification of a novel protease named STAP produced from the strain Streptomyces koyangensis TN650 and the biochemical characterization of this enzyme. This strain was newly isolated from a petroleum sample of Mahres. The purification techniques used in this work led to a homogeneous enzymatic solution having a molecular mass of 45125.17 Da determined by mass spectrometry (MALDI-TOF / MS). Its purity was also verified by the sequencing of its NH2-terminal end (27aa), which shows strong homology with serine proteases of Streptomyces. The optimum of the protease activity is obtained at pH 10 and at 70 ° C on casein, this enzyme remains practically stable at basic pH (7-10) for 120 h. It is an enzyme belonging to the family of thiol-dependent serine proteases because it is essentially inhibited by PMSF and DFP, on the one hand, and DTNP, NEM, iodoacetamide, DTT and 2 -ME, on the other hand. Its thermoactivity and thermostability are considerably improved by calcium at 3 mM. ST AP is characterized by a high specificity with respect to substrates. ST AP, is a good candidate in peptide synthesis because it shows a good activity, stability and tolerance in the presence of various organic solvents at 50% (v / v), in particular in the presence of isopropanol, DMF, chloroform and n-heptane. The STAP enzyme also has remarkable stability in the presence of surfactants (SDS and LAS), surfactants (Tween 20, Tween 80 and Triton X-1 OO), bleaching agents (sodium perborate and H102) and some commercial detergents liquids and solids (Tide, Nadif and OMO). Thus, STAP appears to be of interest and could be used in industrial applications as a biological additive in liquid and solid detergents, since it has an optimum pH of alkaline activity. |
| priorityDate | 2015-05-25-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 45.