Immobilization of Thermomyces lanuginosus Lipase in PVA-alginate Beads
Thermomyces lanuginosus lipase was immobilized in PVA-alginate beads, obtaining immobilization % in the range of 94.4-98.4% using PVA concentrations ranging from 11% to 12.5%, and with cross linking times of 45 and 60 min using boric acid. Initial reaction rate was determined in free and immobilized state by hydrolysis of p-nitrophenol palmitate. Operational stability at different pH (4-7), agitation (100-500 r.p.m.), and temperature (40-80 °C) was investigated. Results showed that pH 6 and 7 no considerable loss of enzyme activity or enzyme was observed. At temperatures over 70 °C, enzyme suffers physical damage and showed a considerable loss of activity. No significant difference was observed when agitation was varied from 100 to 500 r.p.m.
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Sociedad Química de México A.C.
2011
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oai:scielo:S1870-249X20110003000082013-04-17Immobilization of Thermomyces lanuginosus Lipase in PVA-alginate BeadsCruz-Ortiz,Brenda RogelinaRíos-González,Leopoldo JavierGarza García,YolandaRodríguez de la Garza,José AntonioRodríguez-Martínez,Jesús lipase immobilized PVA-alginate Thermomyces lanuginosus Thermomyces lanuginosus lipase was immobilized in PVA-alginate beads, obtaining immobilization % in the range of 94.4-98.4% using PVA concentrations ranging from 11% to 12.5%, and with cross linking times of 45 and 60 min using boric acid. Initial reaction rate was determined in free and immobilized state by hydrolysis of p-nitrophenol palmitate. Operational stability at different pH (4-7), agitation (100-500 r.p.m.), and temperature (40-80 °C) was investigated. Results showed that pH 6 and 7 no considerable loss of enzyme activity or enzyme was observed. At temperatures over 70 °C, enzyme suffers physical damage and showed a considerable loss of activity. No significant difference was observed when agitation was varied from 100 to 500 r.p.m.info:eu-repo/semantics/openAccessSociedad Química de México A.C.Journal of the Mexican Chemical Society v.55 n.3 20112011-09-01info:eu-repo/semantics/articletext/htmlhttp://www.scielo.org.mx/scielo.php?script=sci_arttext&pid=S1870-249X2011000300008en |
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Cruz-Ortiz,Brenda Rogelina Ríos-González,Leopoldo Javier Garza García,Yolanda Rodríguez de la Garza,José Antonio Rodríguez-Martínez,Jesús |
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Cruz-Ortiz,Brenda Rogelina Ríos-González,Leopoldo Javier Garza García,Yolanda Rodríguez de la Garza,José Antonio Rodríguez-Martínez,Jesús Immobilization of Thermomyces lanuginosus Lipase in PVA-alginate Beads |
| author_facet |
Cruz-Ortiz,Brenda Rogelina Ríos-González,Leopoldo Javier Garza García,Yolanda Rodríguez de la Garza,José Antonio Rodríguez-Martínez,Jesús |
| author_sort |
Cruz-Ortiz,Brenda Rogelina |
| title |
Immobilization of Thermomyces lanuginosus Lipase in PVA-alginate Beads |
| title_short |
Immobilization of Thermomyces lanuginosus Lipase in PVA-alginate Beads |
| title_full |
Immobilization of Thermomyces lanuginosus Lipase in PVA-alginate Beads |
| title_fullStr |
Immobilization of Thermomyces lanuginosus Lipase in PVA-alginate Beads |
| title_full_unstemmed |
Immobilization of Thermomyces lanuginosus Lipase in PVA-alginate Beads |
| title_sort |
immobilization of thermomyces lanuginosus lipase in pva-alginate beads |
| description |
Thermomyces lanuginosus lipase was immobilized in PVA-alginate beads, obtaining immobilization % in the range of 94.4-98.4% using PVA concentrations ranging from 11% to 12.5%, and with cross linking times of 45 and 60 min using boric acid. Initial reaction rate was determined in free and immobilized state by hydrolysis of p-nitrophenol palmitate. Operational stability at different pH (4-7), agitation (100-500 r.p.m.), and temperature (40-80 °C) was investigated. Results showed that pH 6 and 7 no considerable loss of enzyme activity or enzyme was observed. At temperatures over 70 °C, enzyme suffers physical damage and showed a considerable loss of activity. No significant difference was observed when agitation was varied from 100 to 500 r.p.m. |
| publisher |
Sociedad Química de México A.C. |
| publishDate |
2011 |
| url |
http://www.scielo.org.mx/scielo.php?script=sci_arttext&pid=S1870-249X2011000300008 |
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