Hydrophobic interaction chromatography as separation method of alkaline proteases from viscera of Scomberomorus sierra
This study focused on recovering alkaline proteases from the viscera of Scomberomorus sierra through hydrophobic interaction chromatography. Three alkaline proteases were partially separated using this chromatographic technique; two of them, with molecular weights of 19 and 31 kDa, were identified a...
| Autores: | , , , , , , |
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| Tipo de documento: | artigo |
| Estado: | Versão publicada |
| Data de publicação: | 2019 |
| País: | México |
| Recursos: | UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO |
| Repositório: | TIP Revista especializada en ciencias químico-biológicas |
| Idioma: | espanhol |
| OAI Identifier: | oai:ojs.ojs.escire.net:article/183 |
| Acesso em linha: | http://tip.zaragoza.unam.mx/index.php/tip/article/view/183 |
| Access Level: | Acceso aberto |
| Palavra-chave: | chymotrypsin; hydrophobic interaction chromatography; Scomberomorus sierra; trypsin quimiotripsina; cromatografía de interacción hidrofóbica; Scomberomorus sierra; tripsina |
| Resumo: | This study focused on recovering alkaline proteases from the viscera of Scomberomorus sierra through hydrophobic interaction chromatography. Three alkaline proteases were partially separated using this chromatographic technique; two of them, with molecular weights of 19 and 31 kDa, were identified as trypsin-like enzymes according to inhibition assays. The 31 kDa alkaline protease, the only isolated enzyme, was purified under following chromatographic conditions: ammonium sulfate 13% (w/v) and ethylene glycol 27% (w/v); this enzyme showed maximum activity at pH 9 – 10 and 50 – 60 °C and was strongly inhibited by soybean trypsin inhibitor (SBTI) and porcine trypsin inhibitor (TPI). A third alkaline protease with molecular weight of 20 kDa was partially separated and inhibited by tosyl phenylalanyl chloromethyl ketone (TPCK), showing optimum activity at pH 9 – 11 and 60 °C. These results show that the viscera of Scomberomorus sierra may be useful as source of proteases. |
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