{"corpus_id":31495828,"paper_sha":"d84b24afc4767324c3395e124e04b6e7b2c34dfe","doi":"10.1111/J.1470-8744.1993.TB00249.X","arxiv_id":null,"pmid":8338641,"pmcid":null,"mag_id":1486949777,"dblp_id":null,"acl_id":null,"title":"Ferulic acid esterase from Aspergillus niger: purification and partial characterization of two forms from a commercial source of pectinase","year":1993,"publication_date":"1993-06-01","venue":"Biotechnology and applied biochemistry","journal":{"name":"Biotechnology and Applied Biochemistry","pages":null,"volume":"17"},"journal_issn":null,"journal_title":null,"publication_types":["JournalArticle"],"pubmed_pub_types":["Journal Article","Research Support, Non-U.S. Gov't"],"s2_fields_of_study":["Biology","Medicine","Chemistry"],"reference_count":0,"citation_count":96,"influential_citation_count":3,"is_open_access":false,"arxiv_categories":null,"arxiv_license":null,"arxiv_journal_ref":null,"mesh_headings":[{"d":"Aspergillus niger","mj":false,"qs":[{"q":"enzymology","mj":true,"ui":"Q000201"}],"ui":"D001234"},{"d":"Carboxylic Ester Hydrolases","mj":false,"qs":[{"q":"chemistry","mj":false,"ui":"Q000737"},{"q":"isolation & purification","mj":true,"ui":"Q000302"},{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D002265"},{"d":"Chromatography, Liquid","mj":false,"qs":[{"q":"methods","mj":false,"ui":"Q000379"}],"ui":"D002853"},{"d":"Isoelectric Focusing","mj":false,"ui":"D007525"},{"d":"Molecular Weight","mj":false,"ui":"D008970"},{"d":"Polygalacturonase","mj":false,"qs":[{"q":"chemistry","mj":true,"ui":"Q000737"}],"ui":"D011096"},{"d":"Substrate Specificity","mj":false,"ui":"D013379"}],"chemicals":[{"n":"Carboxylic Ester Hydrolases","ui":"D002265","reg":"EC 3.1.1.-"},{"n":"feruloyl esterase","ui":"C070196","reg":"EC 3.1.1.73"},{"n":"Polygalacturonase","ui":"D011096","reg":"EC 3.2.1.15"}],"comments_corrections":null,"source_flags":5,"s2_open_access_pdf_url":null,"s2_open_access_landing_url":null,"s2_open_access_license":null,"s2_open_access_status":null,"pmc_open_access_pdf_url":null,"pmc_open_access_landing_url":null,"pmc_open_access_license":null,"pmc_open_access_status":null,"unpaywall_open_access_pdf_url":null,"unpaywall_open_access_landing_url":null,"unpaywall_open_access_license":null,"unpaywall_open_access_status":null,"abstract":"Two forms of ferulic acid esterase from Aspergillus niger have been isolated from a commercial source of pectinase. One, designated I, has a M(r) of 132,000, is probably dimeric, and has a pI of 3.0. The second, designated II, was partially purified and is monomeric (M(r) 29,000), with a pI of 3.6. Both enzymes were free of pectinase and xylanase activity and released ferulic acid from methyl ferulate. In association with a xylanase, they also released ferulic acid from destarched wheat bran. Ferulic acid esterase II released a small amount of ferulic acid (0.09 unit/mg of protein) in the absence of xylanase. The enzymes had different specificities for a range of methyl ester derivatives of cinnamoyl and benzoyl acids, acetylated xylan and p‐nitrophenyl acetate.","claims":[{"public_id":"cl_e9bd018745b983ba203863943daa9412","status":"active","text":"Both enzymes were free of pectinase and xylanase activity and released ferulic acid from methyl ferulate.","confidence":0.97,"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["extraction"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"url":"https://sah.borca.ai/claims/cl_e9bd018745b983ba203863943daa9412"},{"public_id":"cl_ee84be49ca3b99bd2e73dedb991de4dc","status":"active","text":"Ferulic acid esterase I is likely dimeric, has an estimated molecular mass of 132,000, and has a pI of 3.0.","confidence":0.96,"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["extraction"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"url":"https://sah.borca.ai/claims/cl_ee84be49ca3b99bd2e73dedb991de4dc"},{"public_id":"cl_3c86e92a68362997e89798ef84d51c40","status":"active","text":"Ferulic acid esterase II is monomeric, has an estimated molecular mass of 29,000, and has a pI of 3.6.","confidence":0.96,"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["extraction"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"url":"https://sah.borca.ai/claims/cl_3c86e92a68362997e89798ef84d51c40"},{"public_id":"cl_cf1d2885678f5f34061435af231f92ed","status":"active","text":"In combination with xylanase, both enzymes also released ferulic acid from destarched wheat bran, and ferulic acid esterase II released a small amount of ferulic acid without xylanase.","confidence":0.95,"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["extraction"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"url":"https://sah.borca.ai/claims/cl_cf1d2885678f5f34061435af231f92ed"},{"public_id":"cl_53053e84f7ee5f011b79bf862bdba695","status":"active","text":"The two enzymes showed different specificities toward methyl ester derivatives of cinnamoyl and benzoyl acids, acetylated xylan, and p-nitrophenyl acetate.","confidence":0.92,"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["extraction"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"url":"https://sah.borca.ai/claims/cl_53053e84f7ee5f011b79bf862bdba695"},{"public_id":"cl_1e31bec6a64193cf0e70c59d1b24adb2","status":"active","text":"Two forms of ferulic acid esterase were isolated from a commercial pectinase source.","confidence":0.98,"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous 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