Occurrence of ɛ-poly-l-lysine-degrading enzyme in ?-poly-l-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization
Abstract ɛ-Poly-l-lysine (ɛ-PL)-degrading enzyme was found in the ɛ-PL-tolerant strain Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of ɛ-PL and released l-lysine. The enzyme w...
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| Veröffentlicht in: | FEMS microbiology letters 2002-02, Vol.207 (2), p.147-151 |
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| container_end_page | 151 |
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| container_issue | 2 |
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| container_title | FEMS microbiology letters |
| container_volume | 207 |
| creator | Kito, Mitsuaki Onji, Yuichi Yoshida, Toyokazu Nagasawa, Toru |
| description | Abstract
ɛ-Poly-l-lysine (ɛ-PL)-degrading enzyme was found in the ɛ-PL-tolerant strain Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of ɛ-PL and released l-lysine. The enzyme was a Co2+ or Ca2+ ion-activated aminopeptidase. |
| doi_str_mv | 10.1111/j.1574-6968.2002.tb11043.x |
| format | Article |
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ɛ-Poly-l-lysine (ɛ-PL)-degrading enzyme was found in the ɛ-PL-tolerant strain Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of ɛ-PL and released l-lysine. The enzyme was a Co2+ or Ca2+ ion-activated aminopeptidase.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2002.tb11043.x</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Aminopeptidase ; Calcium ; Calcium ions ; Carbon dioxide ; Cobalt ; Degradation ; Enzymes ; Lysine ; Microbiology ; Poly-L-lysine ; Purification ; Sphingobacterium</subject><ispartof>FEMS microbiology letters, 2002-02, Vol.207 (2), p.147-151</ispartof><rights>2002 Federation of European Microbiological Societies 2002</rights><rights>2002 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids></links><search><creatorcontrib>Kito, Mitsuaki</creatorcontrib><creatorcontrib>Onji, Yuichi</creatorcontrib><creatorcontrib>Yoshida, Toyokazu</creatorcontrib><creatorcontrib>Nagasawa, Toru</creatorcontrib><title>Occurrence of ɛ-poly-l-lysine-degrading enzyme in ?-poly-l-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization</title><title>FEMS microbiology letters</title><description>Abstract
ɛ-Poly-l-lysine (ɛ-PL)-degrading enzyme was found in the ɛ-PL-tolerant strain Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of ɛ-PL and released l-lysine. The enzyme was a Co2+ or Ca2+ ion-activated aminopeptidase.</description><subject>Aminopeptidase</subject><subject>Calcium</subject><subject>Calcium ions</subject><subject>Carbon dioxide</subject><subject>Cobalt</subject><subject>Degradation</subject><subject>Enzymes</subject><subject>Lysine</subject><subject>Microbiology</subject><subject>Poly-L-lysine</subject><subject>Purification</subject><subject>Sphingobacterium</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNpdkEtOwzAQhi0EEqVwBwvWDh7HebFBqOKpSl3QveXaTusqtYOToLaX4ACciFuR0qoLZjOjfz7NSB9C10Aj6Ot2GUGScZIWaR4xSlnUzgAoj6P1CRocV6doQOMsJ0CL7BxdNM2SUsoZTQfoa6JUF4JxymBf4p9vUvtqQypSbRrrDNFmHqS2bo6N225WBluH7_8xra9MkK7F7_WiJ_1MqtYE263wqqta--lDP07egN7hugu2tEq21jssncZqIcMe3_6Fl-islFVjrg59iKZPj9PRCxlPnl9HD2PiM84J54lmXOfACxXLAoCbFGKqFcuTWQklNwkzRjMJucoyaRSXKaOz0oDmacF1PEQ3-7N18B-daVqx9F1w_UfBYqBpBlnOeyrZU76rRR3sSoaNACp26sVSHP2KnXpxUC_W8S-zqXwW</recordid><startdate>20020201</startdate><enddate>20020201</enddate><creator>Kito, Mitsuaki</creator><creator>Onji, Yuichi</creator><creator>Yoshida, Toyokazu</creator><creator>Nagasawa, Toru</creator><general>Blackwell Publishing Ltd</general><general>Oxford University Press</general><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope></search><sort><creationdate>20020201</creationdate><title>Occurrence of ɛ-poly-l-lysine-degrading enzyme in ?-poly-l-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization</title><author>Kito, Mitsuaki ; 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ɛ-Poly-l-lysine (ɛ-PL)-degrading enzyme was found in the ɛ-PL-tolerant strain Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of ɛ-PL and released l-lysine. The enzyme was a Co2+ or Ca2+ ion-activated aminopeptidase.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><doi>10.1111/j.1574-6968.2002.tb11043.x</doi><tpages>5</tpages></addata></record> |
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| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 2002-02, Vol.207 (2), p.147-151 |
| issn | 0378-1097 1574-6968 |
| language | eng |
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| source | Oxford University Press Journals; Wiley Online Library; Alma/SFX Local Collection |
| subjects | Aminopeptidase Calcium Calcium ions Carbon dioxide Cobalt Degradation Enzymes Lysine Microbiology Poly-L-lysine Purification Sphingobacterium |
| title | Occurrence of ɛ-poly-l-lysine-degrading enzyme in ?-poly-l-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization |
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