| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_8a61819f74c5bf0dd84fee93678b81d5 |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2319-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/Y02W30-62 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P7-18
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P7-44
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-18
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y301-01074
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/B09B3-60 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-55
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/B09B3-60
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-18
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P7-44
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P7-18 |
| filingDate |
2022-05-19-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_0b2cbf31061c1e0011cef786a8a01c27
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_114e8f87a99317a16bbbedfd47aa3a4e
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_dec8aee76e5438c67f77fd7bc08b05dc
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f12330f0ac65844b9e6996b941a2ecac |
| publicationDate |
2022-09-02-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
CN-114990090-A |
| titleOfInvention |
A bifunctional fusion protein PETase-MHETase variant |
| abstract |
The invention discloses a bifunctional fusion protein PETase-MHETase variant, the technical solution of which includes the use of wild-type MHETase and PETase as the parent (the amino acid sequences are shown in SEQ ID NO.1 and SEQ ID NO.2), Point mutations were performed in various ways to obtain a variety of PETase variants and MHETase variants. The C-terminus of the MHETase variant and the N-terminus of the PETase variant were then covalently linked with a flexible glycine-serine linker to obtain a variety of PETase-MHETase variants. The obtained various PETase‑MHETase variants can catalyze the degradation of more than 80% of PET powder to terephthalic acid and ethylene glycol at 72 °C for 6 h. |
| priorityDate |
2022-05-19-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |