Výsledky vyhledávání - "Maria Beatriz Espeche Turbay"

Synthesis, properties, and uses of silver nanoparticles obtained from leaf extracts

Autor: Valentina Rey, Claudio D. Borsarelli, Mauro Nicolás Gallucci, Fiorella Tulli, Ana Belén Cisneros, Maria Beatriz Espeche Turbay

In the present chapter, we update and review recent literature discussing the use of harvested leaves and aerial parts of plants as a source of bioactive compounds for the biosynthesis of silver nanoparticles (AgNPs) and explain the synthetic techniq

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9a6995c82266782974adcc902f07aee5
https://doi.org/10.1016/b978-0-12-824508-8.00014-9

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Effect of dye localization and self-interactions on the photosensitized generation of singlet oxygen by rose bengal bound to bovine serum albumin

Autor: Natalia Mariel Argañaraz, Alexis Aspée, Valentina Rey, Claudio D. Borsarelli, Eduardo Lissi, Faustino E. Morán Vieyra, Maria Beatriz Espeche Turbay

Publikováno v: Journal of Photochemistry and Photobiology B: Biology. 141:275-282

The spectroscopic and photophysical properties of rose bengal (RB) encased in bovine serum albumin (BSA) have been examined to evaluate the photosensitized generation of singlet molecular oxygen (1O2). The results show that RB photophysical and photo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd462f4666f6c933c924b5f555468f02
https://doi.org/10.1016/j.jphotobiol.2014.09.014

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Milk-derived angiotensin-I-converting enzymeinhibitory peptides generated by Lactobacillus delbrueckii subsp. lactis CRL 581

Autor: Maria Beatriz Espeche Turbay, Josefina M. Villegas, Elvira Maria Hebert, Gianluca Picariello, Graciela Savoy de Giori, Gianfranco Mamone

Publikováno v: CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Peptidomics 1 (2014): 22–29. doi:10.2478/ped-2014-0002
info:cnr-pdr/source/autori:Villegas JM, Picariello G, Mamone G, Espeche Turbay MB, Savoy de Giori G, Hebert EM/titolo:Milk-derived angiotensin-I-converting enzyme inhibitory peptides generated by Lactobacillus delbrueckii subsp. lactis CRL 581/doi:10.2478%2Fped-2014-0002/rivista:Peptidomics/anno:2014/pagina_da:22/pagina_a:29/intervallo_pagine:22–29/volume:1
Peptidomics, Vol 1, Iss 1 (2014)

Several strains of Lactobacillus helveticus and Lactobacillus delbrueckii subsp. lactis were evaluated for their ability to release angiotensin-I-converting enzyme (ACE) inhibitory peptides from alpha-casein and beta-casein. Casein peptides resulting

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18e8a96e27cae541b28af3a26d2b7ef0
https://www.degruyter.com/view/j/ped.2014.1.issue-1/ped-2014-0002/ped-2014-0002.xml

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Diversity in proteinase specificity of thermophilic lactobacilli as revealed by hydrolysis of dairy and vegetable proteins

Autor: Micaela Pescuma, Graciela Font de Valdez, Graciela Savoy de Giori, Fernanda Mozzi, Elvira Maria Hebert, Maria Beatriz Espeche Turbay

The ability of industrially relevant species of thermophilic lactobacilli strains to hydrolyze proteins from animal (caseins and ß-lactoglobulin) and vegetable (soybean and wheat) sources, as well as the influence of the peptide content of the growt

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96f870542644350c23acbe1441ee3675
http://link.springer.com/journal/253

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Release of the cell-envelope-associated proteinase of Lactobacillus delbrueckii subspecies lactis CRL 581 is dependent upon pH and temperature

Autor: Maria Beatriz Espeche Turbay, Graciela Savoy de Giori, Elvira Maria Hebert

Publikováno v: Journal of agricultural and food chemistry. 57(18)

The cell-envelope-associated proteinase of Lactobacillus delbrueckii subsp. lactis CRL 581 (PrtL) has an essential role in bacterial growth and contributes to the development of the organoleptic properties of hard cheeses and to the release of bioact

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4218e1c6015f6bb5b069cd06018bf59f
https://pubmed.ncbi.nlm.nih.gov/19754175

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