Predicate |
Object |
assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_4f0c7be9d3b8bdc11b8fc87f480f54b2 |
classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y501-03 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12R2001-01 |
classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y501-03 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-90 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P19-02 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P19-24 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-70 |
classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-70 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P19-02 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P19-24 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-90 |
filingDate |
2020-09-25-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_cb7a05c5fee66b7ff984918a4707363f http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_89bf2e022422a5f9cc84e728d2d5243e http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_0e4c9a1e9452e8608378e28b18397bbb http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_a9451164b5b8f2e2a5058ca6577cdc66 |
publicationDate |
2022-09-29-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationNumber |
US-2022307062-A1 |
titleOfInvention |
Allulose epimerase variant, method of producing the same, and method of producing allulose using the same |
abstract |
The present invention provides a novel allulose epimerase variant and various uses thereof, in which glycine (Gly), an amino acid residue at position 216 of the amino acid sequence of wild-type D-allulose 3-epimerase derived from Flavonifractor plautii , is substituted with serine (Ser). The novel allulose epimerase variant according to the present invention has a higher conversion activity of fructose to allulose compared to the wild-type D-allulose 3-epimerase derived from Flavonifractor plautii , and in particular, it has excellent thermal stability under high temperature conditions of 60° C. or higher, so that the enzyme conversion reaction is performed at the industrial level for mass production of allulose to prevent contamination, to shorten production time, and to reduce production cost. |
priorityDate |
2019-12-19-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
type |
http://data.epo.org/linked-data/def/patent/Publication |