%0 Journal Article %1 WOS:000315322700012 %A Albertini, A V P %A Silva, J L %A Freire, V N %A Santos, R P %A Martins, J L %A Cavada, B S %A Cadena, P G %A Neto, P J Rolim %A Pimentel, M C B %A Martinez, C R %A Porto, A L F %A Filho, J L Lima %C PO BOX 564, 1001 LAUSANNE, SWITZERLAND %D 2013 %I ELSEVIER SCIENCE SA %J CHEMICAL ENGINEERING JOURNAL %K Glass-ceramic Immobilization; Invertase} Zinc ashes; fly sulfate; support; {Coal %P 91-96 %R 10.1016/j.cej.2012.10.029 %T Immobilized invertase studies on glass-ceramic support from coal fly ashes %V 214 %X Invertase was covalently immobilized on new coal fly ashes glass-ceramic support with zinc sulfate (GCSZn). The coupling process of proteins was demonstrated by X-ray diffraction (XRD). There was no change in the optimum pH (4.6) but optimum temperature increased from 55 degrees C for free invertase to 60 degrees C for immobilized derivative. The activation energy decreased after immobilization (37.31 +/- 3.40 kJ/mol) in spite of free invertase (51.34 +/- 5.21 kJ/mol). There was an improvement in the Michaelis-Menten constant for sucrose hydrolysis after immobilization being 15 times lower compared to that for free invertase (030 +/- 0.01 mmol). After ten reuses at 25 +/- 2 degrees C, the immobilized invertase lost only 9% of initial activity, but at the optimum temperature (60 degrees C), the activity decrease was about 70%, what it is economically feasible under energetic view point for industrial application. (C) 2012 Elsevier B.V. All rights reserved.

@article{WOS:000315322700012, abstract = {Invertase was covalently immobilized on new coal fly ashes glass-ceramic support with zinc sulfate (GCSZn). The coupling process of proteins was demonstrated by X-ray diffraction (XRD). There was no change in the optimum pH (4.6) but optimum temperature increased from 55 degrees C for free invertase to 60 degrees C for immobilized derivative. The activation energy decreased after immobilization (37.31 +/- 3.40 kJ/mol) in spite of free invertase (51.34 +/- 5.21 kJ/mol). There was an improvement in the Michaelis-Menten constant for sucrose hydrolysis after immobilization being 15 times lower compared to that for free invertase (030 +/- 0.01 mmol). After ten reuses at 25 +/- 2 degrees C, the immobilized invertase lost only 9% of initial activity, but at the optimum temperature (60 degrees C), the activity decrease was about 70%, what it is economically feasible under energetic view point for industrial application. (C) 2012 Elsevier B.V. All rights reserved.}, added-at = {2022-05-23T20:00:14.000+0200}, address = {PO BOX 564, 1001 LAUSANNE, SWITZERLAND}, author = {Albertini, A V P and Silva, J L and Freire, V N and Santos, R P and Martins, J L and Cavada, B S and Cadena, P G and Neto, P J Rolim and Pimentel, M C B and Martinez, C R and Porto, A L F and Filho, J L Lima}, biburl = {https://www.bibsonomy.org/bibtex/201a6204222564f73e16ca3047041eefb/ppgfis_ufc_br}, doi = {10.1016/j.cej.2012.10.029}, interhash = {645a7799cf5f126cc4efaabb671dd7d9}, intrahash = {01a6204222564f73e16ca3047041eefb}, issn = {1385-8947}, journal = {CHEMICAL ENGINEERING JOURNAL}, keywords = {Glass-ceramic Immobilization; Invertase} Zinc ashes; fly sulfate; support; {Coal}, pages = {91-96}, publisher = {ELSEVIER SCIENCE SA}, pubstate = {published}, timestamp = {2022-05-23T20:00:14.000+0200}, title = {Immobilized invertase studies on glass-ceramic support from coal fly ashes}, tppubtype = {article}, volume = 214, year = 2013 }