http://rdf.ncbi.nlm.nih.gov/pubchem/patent/ES-2050068-A1
Outgoing Links
Predicate | Object |
---|---|
assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_7da5c8e8c3e8261efe7e698c7198681b |
classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-20 |
classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-20 |
filingDate | 1992-07-03-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_3028014a5839c919f6c0d5263655e943 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_96094fbd8a3753933c5ad8b9f696b212 |
publicationDate | 1994-05-01-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationNumber | ES-2050068-A1 |
titleOfInvention | PROCEDURE FOR THE PURIFICATION OF TWO ROUGH CANDID LIPASE ISOENZYMES. |
abstract | PROCEDURE FOR THE PURIFICATION OF TWO LIPASE ISOENZYMES FROM CANDIDA RUGOSA. PROCEDURE FOR THE PURIFICATION OF TWO EXTRACELLULAR LIPASES PRESENT IN COMMERCIAL CRUDE LIPASE OF THE YEAST CANDIDA RUGOSA. THE METHOD CONSISTS OF A SINGLE STEP OF HYDROPHOBIC CHROMATOGRAPHY IN AN AGAROSE MATRIX. VERY DIFFERENT ELUTION CONDITIONS ALLOW COMPLETE SEPARATION AND PURIFICATION OF TWO ENZYMES WITH LIPASIC ACTIVITY (LIPASES A AND B) PRESENT IN THE START-UP COMMERCIAL EXTRACT. FOR THIS, A CONCENTRATED BUFFER FROM PH 6 TO 8 IS USED, WITH WHICH A LARGE PART OF THE CONTAMINANTS PRESENT IN THE EXTRACT ARE ELUTED FROM THE COLUMN; THEN WITH THE SAME, MORE DILUTE BUFFER SOLUTION, LIPASE B IS CARRIED OUT. SUBSEQUENTLY, LIPASE A IS ELUTED WITH A DI OR POLYALCOHOL DISSOLVED IN THE DILUTE BUFFER, FROM WHICH SOLUTION, BY CONCENTRATION BY ULTRAFILTRATION AND MOLECULAR EXCLUSION CHROMATOGRAPHY WITH DEXTRAN, IT IS REMOVED THE ALCOHOL. IT IS APPLIED INDUSTRIALLY IN THE PURIFICATION OF ENZYMES. |
priorityDate | 1992-07-03-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 152.