http://rdf.ncbi.nlm.nih.gov/pubchem/patent/TN-2016000165-A1
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_ffc709d60c65e11d0447ab7a08b5c025 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-50 |
| filingDate | 2016-05-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_c15448753c05413fe79cabc8099f02d1 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_3a8c3f7f2e3eac75e1ef8389814d8040 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_3dc4a7eeede8aa1262bcd2ffab173d9d http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_129b3d8153bdc068c878ed440bec73bf http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_cd949f14a7a6f0e169e2e67245c05282 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_702cf851a2ab156261d50885beedd157 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_bd76ff813b45a6a68aa8030fae8ac8a1 |
| publicationDate | 2017-10-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | TN-2016000165-A1 |
| titleOfInvention | Screening, purification and biochemical characterization of a new serine protease called SPTC produced by a strain of Basidiomycete Trametes cingulata CTM 10101 tolerant in the presence of organic solvams and active in washing detergents. |
| abstract | This invention relates to homogenous purification and biochemical characterization of an alkaline serine protease called SPTC produced by Trame tes cingulata CTM 10101. This basidiomycete filamentous fungus was isolated from an effluent sample from the chemical company NPK. . The purified enzyme has a molecular weight estimated at 31 kDa by SOS-PAGE 10% and 31405.16 Da determined by mass spectrometry (MALDITOF / MS). Sequencing of the NH <sub> 2 </ sub> -terminal end (23 amino acids) also proves the purity of this enzyme. It shows some homology with fungal serine proteases. The optimum of the protease activity is obtained at pH 9 and 60 ° C. SPTC is totally inhibited by PMSF and DFP where it is an enzyme belonging to the family of serine proteases. It is stable over a wide range of basic pH (7 to 12) and high temperature (40 to 80 ° C). Its thermoactivity and thermostability are considerably improved by calcium at 2 mM. This serine protease can be used as a bio-additive to the formulation of washing detergents. It is a good candidate for peptide synthesis since it is stable in the presence of organic solvents (50% v / v), in particular hydrophobic solvents, unlike the enzymes found in the bibliography which are more stable in the presence of hydrophilic organic solvents. The SPTC enzyme also shows remarkable stability in the presence of SOS surfactants, surfactants (Tween 20, Tween 80 and Triton X-100), bleaching agents (sodium perborate and H <sub> 2 </ sub> O < sub> 2 </ sub>) and some liquid and solid commercial detergents (EcoVax, Dixan and Skip). Also adding the SPTC protease to the detergent solution improves the performance of the detergent Skip in the direction of better discoloration of blood stains. In addition, the SPTC protease is characterized by a high specificity with regard to protein substrates and is endowed with a better catalytic efficiency by comparing it with commercial proteases: thermolysin type X and Flavourzyme® 500 L. Thus, the SPTC protease appears to respond to the majority of a good protease that provides peptide and bioadditive synthesis in the formulation of liquid and solid washing detergents. |
| priorityDate | 2016-05-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
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