Beatriz Torrestiana-Sanchez

Prof. Beatriz Torrestiana-Sanchez

Tecnológico Nacional de México- Instituto Tecnológico de Veracruz
orcid

Research Focus & Metrics

Academic Career Length

28Years (1999-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 July 2017 in Fuel
Verified
Journal Article
Closed access
VTVeymar Guadalupe Tacias-Pascacio
Veymar Guadalupe Tacias-Pascacio
JVJose J. Virgen-Ortíz
Jose J. Virgen-Ortíz
MJMauricio Jiménez-Pérez
Mauricio Jiménez-Pérez
MYMalcolm Yates
Malcolm Yates
BTBeatriz Torrestiana-Sanchez
Beatriz Torrestiana-Sanchez
Roberto Fernandez-LafuenteRoberto Fernandez-Lafuente
Roberto Fernandez-Lafuente

1 May 2019 in Renewable Energy
Verified
Journal Article
Closed access
VTVeymar Guadalupe Tacias-Pascacio
Veymar Guadalupe Tacias-Pascacio
BTBeatriz Torrestiana-Sanchez
Beatriz Torrestiana-Sanchez
LMLucas Dal Magro
Lucas Dal Magro
JVJose J. Virgen-Ortíz
Jose J. Virgen-Ortíz
FSFrancisco J. Suárez-Ruíz
Francisco J. Suárez-Ruíz
Roberto Fernandez-LafuenteRoberto Fernandez-Lafuente
Roberto Fernandez-Lafuente


17 October 2016 in RSC Advances
Verified
Journal Article
Closed access
PDF file
VTVeymar Guadalupe Tacias-Pascacio
Veymar Guadalupe Tacias-Pascacio
SPSara Peirce
Sara Peirce
BTBeatriz Torrestiana-Sanchez
Beatriz Torrestiana-Sanchez
MYMalcon Yates
Malcon Yates
ARArnulfo Rosales-Quintero
Arnulfo Rosales-Quintero
Roberto Fernandez-LafuenteRoberto Fernandez-Lafuente
Roberto Fernandez-Lafuente
Five different commercial supports (Lifetech™ ECR1061M (styrene/methacrylic polymer), Lifetech™ ECR8804M (octadecyl methacrylate), Lifetech™ ECR8806M (octadecyl methacylate), Lifetech™ ECR1090M (styrene) and Lifetech™ ECR1030M (DVB/methacrylic polymer)) were compared to octyl agarose in their performance in the immobilization of four different lipases (from Rhizomucor miehie (RML), from Thermomyces lanuginosus (TLL) and the forms A and B from Candida antarctica, (CALA and CALB)) and of the phospholipase Lecitase Ultra™ (LU). The new enzymatic derivatives were evaluated and compared with the commercial biocatalyst (Novozym 435 (CALB), Lipozyme RM IM and Lipozyme TL IM). Textural properties, loading capacity, enzyme stability under different conditions, and activity versus different substrates were analyzed. Although all of the supports reversibly immobilized lipases via interfacial activation of lipases versus the hydrophobic surface of the support, some of them permitted a significant improvement in the final biocatalyst compared to the reference support or the commercial preparations. Enzyme specificity depended strongly on the used support (e.g., the new ones gave almost null activity versus p-nitrophenyl butyrate). However, there is not a universal optimal support; the “best” support depends on the enzyme, the parameter studied and the substrate utilized. Nevertheless, under the conditions utilized, the preparations showed a very good performance in a diversity of reactions and permitted their reuse (both the biocatalyst and the supports after eliminating the enzyme by washing the enzyme with triton X-100). These supports will permit enlarging the library of immobilized lipase biocatalyst, being supports useful for aqueous or organic medium.

9 September 2010 in Journal of Chemical Technology & Biotechnology
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Journal Article
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Benigno Ortiz-MuñizBenigno Ortiz-Muñiz
Benigno Ortiz-Muñiz
OCOctavio Carvajal‐Zarrabal
Octavio Carvajal‐Zarrabal
BTBeatriz Torrestiana-Sanchez
Beatriz Torrestiana-Sanchez
MAMARIA GUADALUPE AGUILAR-USCANGA
MARIA GUADALUPE AGUILAR-USCANGA

1 October 2017 in Chemical Engineering Research and Design
Verified
Journal Article
Closed access
VCVioleta Carpintero-Tepole
Violeta Carpintero-Tepole
EFEdmundo Brito-De la Fuente
Edmundo Brito-De la Fuente
BTBeatriz Torrestiana-Sanchez
Beatriz Torrestiana-Sanchez