Purification and Properties of a Collagenolytic Protease Produced by Marine Bacterium Vibrio vulnificus CYK279H
A collagenolytic enzyme, produced by Vibrio vulnificus CYK279H, was purified by ultrafiltration, dialysis, Q-Sepharose ion exchange and Superdex-200 gel chromatography. The enzyme from the supernatant was purified 13.2 fold, with a yield of 11.4%. The molecular weight of the purified enzyme was esti...
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| Veröffentlicht in: | Biotechnology and bioprocess engineering 2005-11, Vol.10 (6) |
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| creator | Kang, S.I. (Pukyong National University, Busan, Republic of Korea) Jang, Y.B. (Pukyong National University, Busan, Republic of Korea) Choi, Y.J. (Gyeongsang National University, Jinju, Republic of Korea) Kong, J.Y. (Pukyong National University, Busan, Republic of Korea), E-mail: kongjy@pknu.ac.kr |
| description | A collagenolytic enzyme, produced by Vibrio vulnificus CYK279H, was purified by ultrafiltration, dialysis, Q-Sepharose ion exchange and Superdex-200 gel chromatography. The enzyme from the supernatant was purified 13.2 fold, with a yield of 11.4%. The molecular weight of the purified enzyme was estimated by SDS-PAGE to be approximately 35.0 kDa. The N-terminal sequence of the enzyme was determined as Gly-Asp-Pro-Cys-Met-Pro-Ile-Ile-Ser-Asn. The optimum temperature and pH for the enzyme activity were 35℃ and 7.5, respectively. |
| doi_str_mv | 10.1007/BF02932300 |
| format | Article |
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(Pukyong National University, Busan, Republic of Korea) ; Jang, Y.B. (Pukyong National University, Busan, Republic of Korea) ; Choi, Y.J. (Gyeongsang National University, Jinju, Republic of Korea) ; Kong, J.Y. (Pukyong National University, Busan, Republic of Korea), E-mail: kongjy@pknu.ac.kr</creator><creatorcontrib>Kang, S.I. (Pukyong National University, Busan, Republic of Korea) ; Jang, Y.B. (Pukyong National University, Busan, Republic of Korea) ; Choi, Y.J. (Gyeongsang National University, Jinju, Republic of Korea) ; Kong, J.Y. (Pukyong National University, Busan, Republic of Korea), E-mail: kongjy@pknu.ac.kr</creatorcontrib><description>A collagenolytic enzyme, produced by Vibrio vulnificus CYK279H, was purified by ultrafiltration, dialysis, Q-Sepharose ion exchange and Superdex-200 gel chromatography. The enzyme from the supernatant was purified 13.2 fold, with a yield of 11.4%. The molecular weight of the purified enzyme was estimated by SDS-PAGE to be approximately 35.0 kDa. The N-terminal sequence of the enzyme was determined as Gly-Asp-Pro-Cys-Met-Pro-Ile-Ile-Ser-Asn. The optimum temperature and pH for the enzyme activity were 35℃ and 7.5, respectively.</description><identifier>ISSN: 1226-8372</identifier><identifier>EISSN: 1976-3816</identifier><identifier>DOI: 10.1007/BF02932300</identifier><language>eng</language><subject>GELATIN ; GELATINA ; GELATINE ; metalloprotease ; PROTEASAS ; PROTEASE ; PROTEASES ; PURIFICACION ; PURIFICATION ; VIBRIO VULNIFICUS</subject><ispartof>Biotechnology and bioprocess engineering, 2005-11, Vol.10 (6)</ispartof><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>Kang, S.I. (Pukyong National University, Busan, Republic of Korea)</creatorcontrib><creatorcontrib>Jang, Y.B. (Pukyong National University, Busan, Republic of Korea)</creatorcontrib><creatorcontrib>Choi, Y.J. (Gyeongsang National University, Jinju, Republic of Korea)</creatorcontrib><creatorcontrib>Kong, J.Y. (Pukyong National University, Busan, Republic of Korea), E-mail: kongjy@pknu.ac.kr</creatorcontrib><title>Purification and Properties of a Collagenolytic Protease Produced by Marine Bacterium Vibrio vulnificus CYK279H</title><title>Biotechnology and bioprocess engineering</title><description>A collagenolytic enzyme, produced by Vibrio vulnificus CYK279H, was purified by ultrafiltration, dialysis, Q-Sepharose ion exchange and Superdex-200 gel chromatography. The enzyme from the supernatant was purified 13.2 fold, with a yield of 11.4%. The molecular weight of the purified enzyme was estimated by SDS-PAGE to be approximately 35.0 kDa. The N-terminal sequence of the enzyme was determined as Gly-Asp-Pro-Cys-Met-Pro-Ile-Ile-Ser-Asn. The optimum temperature and pH for the enzyme activity were 35℃ and 7.5, respectively.</description><subject>GELATIN</subject><subject>GELATINA</subject><subject>GELATINE</subject><subject>metalloprotease</subject><subject>PROTEASAS</subject><subject>PROTEASE</subject><subject>PROTEASES</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>VIBRIO VULNIFICUS</subject><issn>1226-8372</issn><issn>1976-3816</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNotj9FLwzAYxIMoOKcvvgv5B6pfkjZJH11RJ5s4RAWfxpcmGZHaSNIK--_t0Kf7wR13HCGXDK4ZgLpZ3AOvBRcAR2TGaiULoZk8nphzWWih-Ck5y_kToFRa6xmJmzEFH1ocQuwp9pZuUvx2aQgu0-gp0iZ2He5cH7v9ENqDPTjM7gB2bJ2lZk-fMIXe0QW2g0th_KLvwaQQ6c_Y9Yf2MdPmY8VVvTwnJx677C7-dU7e7u9em2Wxfn54bG7XhWdKDUVZmaqypeTeKNRGeY2m1aye9rjD6am1AoVEySpZClY7cEZVYJVXILU0Yk6u_no9xi3uUsjb1QsHkMDkFBC_-L5X6g</recordid><startdate>200511</startdate><enddate>200511</enddate><creator>Kang, S.I. 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(Gyeongsang National University, Jinju, Republic of Korea)</creatorcontrib><creatorcontrib>Kong, J.Y. (Pukyong National University, Busan, Republic of Korea), E-mail: kongjy@pknu.ac.kr</creatorcontrib><collection>AGRIS</collection><jtitle>Biotechnology and bioprocess engineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kang, S.I. (Pukyong National University, Busan, Republic of Korea)</au><au>Jang, Y.B. (Pukyong National University, Busan, Republic of Korea)</au><au>Choi, Y.J. (Gyeongsang National University, Jinju, Republic of Korea)</au><au>Kong, J.Y. 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The optimum temperature and pH for the enzyme activity were 35℃ and 7.5, respectively.</abstract><doi>10.1007/BF02932300</doi></addata></record> |
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| ispartof | Biotechnology and bioprocess engineering, 2005-11, Vol.10 (6) |
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| source | EZB-FREE-00999 freely available EZB journals; SpringerLink Journals - AutoHoldings |
| subjects | GELATIN GELATINA GELATINE metalloprotease PROTEASAS PROTEASE PROTEASES PURIFICACION PURIFICATION VIBRIO VULNIFICUS |
| title | Purification and Properties of a Collagenolytic Protease Produced by Marine Bacterium Vibrio vulnificus CYK279H |
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