Anion exchange resin as support for invertase immobilization
The invertase (EC 3.2.1.26) from Saccharomyces cerevisiae was employed as a model enzyme in the evaluation of the adsorption capacity of DOWEX-1X8-50®, a basic anion exchange resin, when used as support in enzyme immobilization. By mixing 100mg of resin with 27mg of invertase (pI = 4.0) in buffer so...
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| Format: | Article |
| Language: | English |
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São Paulo State University (UNESP)
2005-09-01
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| Series: | Revista de Ciências Farmacêuticas Básica e Aplicada |
| Subjects: | |
| Online Access: | http://rcfba.fcfar.unesp.br/index.php/ojs/article/view/583 |
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| author | R.R. Ribeiro M. Vitolo |
| author_facet | R.R. Ribeiro M. Vitolo |
| author_sort | R.R. Ribeiro |
| collection | DOAJ |
| description | The invertase (EC 3.2.1.26) from Saccharomyces cerevisiae was employed as a model enzyme in the evaluation of the adsorption capacity of DOWEX-1X8-50®, a basic anion exchange resin, when used as support in enzyme immobilization. By mixing 100mg of resin with 27mg of invertase (pI = 4.0) in buffer solution (pH 4.6, 25°C), stirred at 100rpm, an adsorption of 93% was achieved. The activities (1U = amount of enzyme forming 1mg reducing sugars/min) of soluble and insoluble invertase were 0.084 U/mgE and 0.075 U/mgE, respectively, giving an immobilization coefficient of 90.4%. The immobilized invertase had a higher thermal stability than the soluble form. The highest activity was observed at pH 4.5 in both forms of the enzyme, whereas the pH stability ranges for soluble and insoluble invertase were 3.5-5.0 and 4.5-5.5, respectively. The kinetic constants for soluble invertase were K M = 18.3 mM and Vmax = 0.084 U/mgE, and for the insoluble form, KM = 29.1 mM and Vmax = 0.075 U/mgE. The resin tested adsorbed the invertase very well, provided the enzyme molecule had a net negative charge, i.e., the immobilization and reaction procedures had to be carried out at pH > pI. |
| first_indexed | 2024-12-14T00:57:48Z |
| format | Article |
| id | doaj.art-458a41ca35f74cf3bcd9c49183841a99 |
| institution | Directory Open Access Journal |
| issn | 1808-4532 2179-443X |
| language | English |
| last_indexed | 2024-12-14T00:57:48Z |
| publishDate | 2005-09-01 |
| publisher | São Paulo State University (UNESP) |
| record_format | Article |
| series | Revista de Ciências Farmacêuticas Básica e Aplicada |
| spelling | doaj.art-458a41ca35f74cf3bcd9c49183841a992022-12-21T23:23:27ZengSão Paulo State University (UNESP)Revista de Ciências Farmacêuticas Básica e Aplicada1808-45322179-443X2005-09-01263583Anion exchange resin as support for invertase immobilizationR.R. RibeiroM. VitoloThe invertase (EC 3.2.1.26) from Saccharomyces cerevisiae was employed as a model enzyme in the evaluation of the adsorption capacity of DOWEX-1X8-50®, a basic anion exchange resin, when used as support in enzyme immobilization. By mixing 100mg of resin with 27mg of invertase (pI = 4.0) in buffer solution (pH 4.6, 25°C), stirred at 100rpm, an adsorption of 93% was achieved. The activities (1U = amount of enzyme forming 1mg reducing sugars/min) of soluble and insoluble invertase were 0.084 U/mgE and 0.075 U/mgE, respectively, giving an immobilization coefficient of 90.4%. The immobilized invertase had a higher thermal stability than the soluble form. The highest activity was observed at pH 4.5 in both forms of the enzyme, whereas the pH stability ranges for soluble and insoluble invertase were 3.5-5.0 and 4.5-5.5, respectively. The kinetic constants for soluble invertase were K M = 18.3 mM and Vmax = 0.084 U/mgE, and for the insoluble form, KM = 29.1 mM and Vmax = 0.075 U/mgE. The resin tested adsorbed the invertase very well, provided the enzyme molecule had a net negative charge, i.e., the immobilization and reaction procedures had to be carried out at pH > pI.http://rcfba.fcfar.unesp.br/index.php/ojs/article/view/583invertase, immobilization, adsorption, anionexchange resin. |
| spellingShingle | R.R. Ribeiro M. Vitolo Anion exchange resin as support for invertase immobilization Revista de Ciências Farmacêuticas Básica e Aplicada invertase, immobilization, adsorption, anionexchange resin. |
| title | Anion exchange resin as support for invertase immobilization |
| title_full | Anion exchange resin as support for invertase immobilization |
| title_fullStr | Anion exchange resin as support for invertase immobilization |
| title_full_unstemmed | Anion exchange resin as support for invertase immobilization |
| title_short | Anion exchange resin as support for invertase immobilization |
| title_sort | anion exchange resin as support for invertase immobilization |
| topic | invertase, immobilization, adsorption, anionexchange resin. |
| url | http://rcfba.fcfar.unesp.br/index.php/ojs/article/view/583 |
| work_keys_str_mv | AT rrribeiro anionexchangeresinassupportforinvertaseimmobilization AT mvitolo anionexchangeresinassupportforinvertaseimmobilization |