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Saccharomyces cerevisiae (Invertase E1103)

Food additives

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#1 qui

qui

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Posted 19 November 2013 - 03:04 AM

Does anybody know if the Food Additive E1103 in bakery products, remain after the product is baked?

 

I have this additive as ingredient in my product but in Australia is just permitted as Processing Aids, my supplier states that this enzyme disappears once the product is baked, any ideas??

 

Thanks 

 

Quimica


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#2 Ferdi1982

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Posted 22 November 2013 - 11:28 AM

Dear Quimica,

 

Being an enzime, I'm pretty sure it will be rapidly inactivated at baking temperature.Would be more sure knowing the temperature profile of your product inside the baking oven. In any case, it should reach temperatures above 120°C, so no chances for enzimes to keep working...

 

Regards

Ferdi


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#3 qui

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Posted 24 November 2013 - 11:49 PM

thanks Ferdi, the product when being baked reaches 190 celsius degrees for 15 minutes.

 

Do you know any formal published paper or article where this statement about at which temperature  Invertase gets inactivated?

 

Cheers, 

 

Quimica


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#4 Creative86

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Posted 25 November 2013 - 09:22 AM

Hello Quimica,

                     I found the following article on the internet that supports the statement that the invertase enzyme form the source  saccharomyces cerevisiae can be inactivated  45 to 70 °C.

                      

Effect of temperature and pressure on yeast invertase stability: a kinetic and conformational study

  • Dominique Cavaille,
  • Didier Combes
  • INSA, Centre de Bioingénierie Gilbert Durand (URA CNRS 544, LA INRA), Complexe Scientifique de Rangueil, 31077 Toulouse Cedex, France
Abstract

Kinetics of the temperature- or pressure-induced denaturation of invertase from Saccharomyces cerevisiae were obtained in the temperature range 45–70°C and in the pressure range 500–650 MPa. The investigation was done by measuring the residual activities after cooling or pressure release and the intrinsic fluorescence of aromatic amino-acids (tyrosine and tryptophan) upon excitation at 277 nm. The residual activity decreased exponentially as a function of time incubation according to a biphasic model either with pressure or temperature, whereas the fluorescence emission indicated a difference between these two parameters. When the enzyme was subjected to thermal treatment, the fluorescence of tyrosine and tryptophan decreased slowly, while after high-pressure treatment, these aromatic residues become more exposed to the aqueous solvent during unfolding, giving rise to a large decrease in fluorescence in the 330–340 nm region. Moreover, in the latter case, an enhancement of light scattering intensity showed changes in protein-protein interactions.

Keywords

  • Invertase; Irreversible denaturation;High pressure;Thermal deactivation;Intrinsic fluorescence
     

Reference Link: http://www.sciencedi...16816569500145X

 

-Creative


Edited by Creative86, 25 November 2013 - 09:37 AM.

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