| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_10d7eee6f46ba12096f177f1b9990b9c
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_6c314a9b21848c5fd4f8a24a37fe90f9
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_33b7f4a64d03a6f999878bd372644f19
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_46e3fd8c27dd2442166a352dc39689c2
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_133cd5c56778dfbd89aa7fcfaa701621
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_d4cffaf185d3d7a06617971b673c845f |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y301-01011
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-18 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07H21-04
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P19-04
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-10 |
| filingDate |
2007-11-20-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_b92af34a5b0683c4c851f8fc10c1da14
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_4ad0bae09ea5c26f6e9f706e41a3a33f
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_e498ed903ed515d24a33a2d105dee13e
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_672808c8ec20ad576a1696ae493e4307
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_51f97247f2cb8f4671405b460b5abfe8
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_8db03e10f1a63d2c30a516793fefaa8b |
| publicationDate |
2009-05-21-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
US-2009130722-A1 |
| titleOfInvention |
Thermally-tolerant pectin methylesterase |
| abstract |
Enzymes accumulated in plant cell walls serve diverse physiological functions including metabolism, polysaccharide structure modification, and molecular communication in interactions with other organisms. Pectin methylesterases are economically important enzymes for their impact on quality and processing properties of fruit and vegetable food products. We have now purified TT-PME to homogeneity from sweet orange finisher pulp and determined the complete corresponding nucleic acid sequence. Purified TT-PME was observed by SDS-PAGE as two doublet bands with molecular masses of approximately 46,000 Da and 56,000 Da. Direct Edman sequencing from these proteins showed a common N-terminal peptide. De novo sequencing of eight TT-PME tryptic peptides determined by MALDI-TOF/TOF mass spectrometry provided additional internal sequences. TT-PME did not correspond to any previously reported Citrus spp. PME sequence. Our results show Citrus TT-PME is a distinctive new isoform with phylogenetic relationship closer to PME isoforms in other species rather than to previously described Citrus PME genes. |
| isCitedBy |
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-104483374-A |
| priorityDate |
2007-11-20-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |