http://rdf.ncbi.nlm.nih.gov/pubchem/patent/BR-102014013453-A2

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assignee http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_448f8c8c395bc367f28833558250f22f
classificationIPCAdditional http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-685
classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/B09B3-60
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P1-02
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filingDate 2014-05-26-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_af23f58145324f6b902550cdaf736a8d
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_014df1686303fa0e9b2833573ec79173
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publicationDate 2016-04-05-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber BR-102014013453-A2
titleOfInvention method for the production of aspergillus niger lipase using mangaba pulp processing residues as substrate
abstract method for the production of aspergillus niger lipase using mangaba pulp processing residues as substrate. The present invention is the production of aspergillus niger lipase from solid state fermentation of mangaba pulp processing residues. The innovation of the work was the use of this waste from the sergipe fruit pulp processing industry, commonly discarded in garbage or destined to feed pigs. The residue, which was used as the sole source of nutrients, as it has a significant amount of lipids in its composition induces enzyme production during fermentation by the microorganism without the need to add any oil as inducer. The lipase obtained showed good thermal stability at temperatures of 37 ° C, 50 ° C and 55 ° C, at the optimum pH of 5.0, and may have the potential to be used as a biocatalyst in lipid modification reactions (hydrolysis, interesterification or esterification). where temperatures up to 55 ° C are required.
isCitedBy http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-109776686-A
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priorityDate 2014-05-26-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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