Purification and Characterization of an Endopeptidase from Propionibacterium freudenreichii
A 44-kDa endopeptidase, isolated by lysozyme and sonic treatment from the cytoplasm of Propionibacterium freudenreichii ATCC 9614, was purified to homogeneity. Ion-exchange chromatography of the cytoplasmic fraction separated the enzyme from several fractions with caseinolytic activities and one fra...
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| Veröffentlicht in: | Journal of dairy science 1996-12, Vol.79 (12), p.2129-2136 |
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| creator | Tobiassen, R.O. Pripp, A.H. Stepaniak, L. Sørhaug, T. |
| description | A 44-kDa endopeptidase, isolated by lysozyme and sonic treatment from the cytoplasm of Propionibacterium freudenreichii ATCC 9614, was purified to homogeneity. Ion-exchange chromatography of the cytoplasmic fraction separated the enzyme from several fractions with caseinolytic activities and one fraction with proline iminopeptidase activity. The endopeptidase was subsequently purified by chromatography and by gel filtration. The enzyme was a monomer with a pI of 3.8, and the enzyme hydrolyzed bradykinin most actively between pH 6.5 and 8 and between 45 and 50°C. The specificity of the Propionibacterium endopeptidase on bradykinin, methionine enkephalin, angiotensin I, and αs1-CN (f1-23) was determined; specificity on αs1-CN (f1-23) was different from that of the 70-kDa endopeptidase (PepO) from Lactococcus spp. The activity on oxidized insulin β-chain was very low. The enzyme was inhibited more by EDTA than by 1,10-phenanthroline and was not sensitive to phosphoramidon. |
| doi_str_mv | 10.3168/jds.S0022-0302(96)76587-6 |
| format | Article |
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Ion-exchange chromatography of the cytoplasmic fraction separated the enzyme from several fractions with caseinolytic activities and one fraction with proline iminopeptidase activity. The endopeptidase was subsequently purified by chromatography and by gel filtration. The enzyme was a monomer with a pI of 3.8, and the enzyme hydrolyzed bradykinin most actively between pH 6.5 and 8 and between 45 and 50°C. The specificity of the Propionibacterium endopeptidase on bradykinin, methionine enkephalin, angiotensin I, and αs1-CN (f1-23) was determined; specificity on αs1-CN (f1-23) was different from that of the 70-kDa endopeptidase (PepO) from Lactococcus spp. The activity on oxidized insulin β-chain was very low. The enzyme was inhibited more by EDTA than by 1,10-phenanthroline and was not sensitive to phosphoramidon.</description><identifier>ISSN: 0022-0302</identifier><identifier>EISSN: 1525-3198</identifier><identifier>DOI: 10.3168/jds.S0022-0302(96)76587-6</identifier><identifier>CODEN: JDSCAE</identifier><language>eng</language><publisher>Savoy, IL: Elsevier Inc</publisher><subject>acide amine ; actividad enzimatica ; activite enzymatique ; amino acids ; aminoacidos ; analytical methods ; Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; casein ; caseina ; caseine ; cheese ; cinina ; endopeptidase ; enzymic activity ; Fundamental and applied biological sciences. Psychology ; kinine ; kinins ; Mission oriented research ; molecular weight ; peptidasas ; peptidase ; peptidases ; peptide ; peptides ; peptidos ; peso molecular ; Physiology and metabolism ; poids moleculaire ; propionibacterium ; Propionibacterium sp ; proteinas ; proteine ; proteins ; purificacion ; purification ; technique analytique ; tecnicas analiticas ; temperatura ; temperature</subject><ispartof>Journal of dairy science, 1996-12, Vol.79 (12), p.2129-2136</ispartof><rights>1996 American Dairy Science Association</rights><rights>1997 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c482t-fcf15808d99b8e4f039acf3889ec4e266353a0dd57c1b764f84dc98c5251219a3</citedby><cites>FETCH-LOGICAL-c482t-fcf15808d99b8e4f039acf3889ec4e266353a0dd57c1b764f84dc98c5251219a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.3168/jds.S0022-0302(96)76587-6$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3548,27868,27923,27924,45994</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2539679$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Tobiassen, R.O.</creatorcontrib><creatorcontrib>Pripp, A.H.</creatorcontrib><creatorcontrib>Stepaniak, L.</creatorcontrib><creatorcontrib>Sørhaug, T.</creatorcontrib><creatorcontrib>Agricultural University of Norway, As, Norway</creatorcontrib><title>Purification and Characterization of an Endopeptidase from Propionibacterium freudenreichii</title><title>Journal of dairy science</title><description>A 44-kDa endopeptidase, isolated by lysozyme and sonic treatment from the cytoplasm of Propionibacterium freudenreichii ATCC 9614, was purified to homogeneity. Ion-exchange chromatography of the cytoplasmic fraction separated the enzyme from several fractions with caseinolytic activities and one fraction with proline iminopeptidase activity. The endopeptidase was subsequently purified by chromatography and by gel filtration. The enzyme was a monomer with a pI of 3.8, and the enzyme hydrolyzed bradykinin most actively between pH 6.5 and 8 and between 45 and 50°C. The specificity of the Propionibacterium endopeptidase on bradykinin, methionine enkephalin, angiotensin I, and αs1-CN (f1-23) was determined; specificity on αs1-CN (f1-23) was different from that of the 70-kDa endopeptidase (PepO) from Lactococcus spp. The activity on oxidized insulin β-chain was very low. The enzyme was inhibited more by EDTA than by 1,10-phenanthroline and was not sensitive to phosphoramidon.</description><subject>acide amine</subject><subject>actividad enzimatica</subject><subject>activite enzymatique</subject><subject>amino acids</subject><subject>aminoacidos</subject><subject>analytical methods</subject><subject>Biological and medical sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biotechnology</subject><subject>casein</subject><subject>caseina</subject><subject>caseine</subject><subject>cheese</subject><subject>cinina</subject><subject>endopeptidase</subject><subject>enzymic activity</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>kinine</topic><topic>kinins</topic><topic>Mission oriented research</topic><topic>molecular weight</topic><topic>peptidasas</topic><topic>peptidase</topic><topic>peptidases</topic><topic>peptide</topic><topic>peptides</topic><topic>peptidos</topic><topic>peso molecular</topic><topic>Physiology and metabolism</topic><topic>poids moleculaire</topic><topic>propionibacterium</topic><topic>Propionibacterium sp</topic><topic>proteinas</topic><topic>proteine</topic><topic>proteins</topic><topic>purificacion</topic><topic>purification</topic><topic>technique analytique</topic><topic>tecnicas analiticas</topic><topic>temperatura</topic><topic>temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tobiassen, R.O.</creatorcontrib><creatorcontrib>Pripp, A.H.</creatorcontrib><creatorcontrib>Stepaniak, L.</creatorcontrib><creatorcontrib>Sørhaug, T.</creatorcontrib><creatorcontrib>Agricultural University of Norway, As, Norway</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Periodicals Index Online Segment 50</collection><collection>Periodicals Index Online</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - 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Ion-exchange chromatography of the cytoplasmic fraction separated the enzyme from several fractions with caseinolytic activities and one fraction with proline iminopeptidase activity. The endopeptidase was subsequently purified by chromatography and by gel filtration. The enzyme was a monomer with a pI of 3.8, and the enzyme hydrolyzed bradykinin most actively between pH 6.5 and 8 and between 45 and 50°C. The specificity of the Propionibacterium endopeptidase on bradykinin, methionine enkephalin, angiotensin I, and αs1-CN (f1-23) was determined; specificity on αs1-CN (f1-23) was different from that of the 70-kDa endopeptidase (PepO) from Lactococcus spp. The activity on oxidized insulin β-chain was very low. The enzyme was inhibited more by EDTA than by 1,10-phenanthroline and was not sensitive to phosphoramidon.</abstract><cop>Savoy, IL</cop><pub>Elsevier Inc</pub><doi>10.3168/jds.S0022-0302(96)76587-6</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of dairy science, 1996-12, Vol.79 (12), p.2129-2136 |
| issn | 0022-0302 1525-3198 |
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| source | Periodicals Index Online; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals |
| subjects | acide amine actividad enzimatica activite enzymatique amino acids aminoacidos analytical methods Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology casein caseina caseine cheese cinina endopeptidase enzymic activity Fundamental and applied biological sciences. Psychology kinine kinins Mission oriented research molecular weight peptidasas peptidase peptidases peptide peptides peptidos peso molecular Physiology and metabolism poids moleculaire propionibacterium Propionibacterium sp proteinas proteine proteins purificacion purification technique analytique tecnicas analiticas temperatura temperature |
| title | Purification and Characterization of an Endopeptidase from Propionibacterium freudenreichii |
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