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.
%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
}