Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Amelia Farrés"'
Publikováno v:
Polymers, Vol 16, Iss 14, p 1994 (2024)
Poly(lactic-acid) (PLA) is a biodegradable polymer widely used as a packaging material. Its monomer, lactic acid, and its derivatives have been used in the food, cosmetic, and chemical industries. The accumulation of PLA residues leads to the develop
Externí odkaz:
https://doaj.org/article/a3fc3bf9607f4c7da6210b107a99a741
Publikováno v:
Catalysts, Vol 13, Iss 3, p 591 (2023)
The enzymatic degradation of the recalcitrant poly(ethylene terephthalate) (PET) has been an important biotechnological goal. The present review focuses on the state of the art in enzymatic degradation of PET, and the challenges ahead. This review co
Externí odkaz:
https://doaj.org/article/cf9c139bb60341d78156a9462ff9ad2b
Autor:
Silvia Armenta, Zaira Sánchez-Cuapio, Amelia Farrés, Karen Manoutcharian, Alejandra Hernandez-Santoyo, Sergio Sánchez, Romina Rodríguez-Sanoja
Publikováno v:
Data in Brief, Vol 21, Iss , Pp 1944-1949 (2018)
Carbohydrate-binding modules (CBMs) are auxiliary domains into glycoside-hydrolases that allow the interaction between the insoluble substrate and the solubilized enzyme, through hydrophobic, CH-π interactions and hydrogen bonds. Here, we present th
Externí odkaz:
https://doaj.org/article/c43e3a91fe784dc1b3d7d3fdd43d6e14
Publikováno v:
TIP Revista Especializada en Ciencias Químico-Biológicas, Vol 13, Iss 1, Pp 16-25 (2010)
Las cutinasas (EC 3.1.1.74) son enzimas que catalizan la hidrólisis del polímero lipídico cutina, un componente estructural de la cutícula de las plantas. Estas enzimas muestran propiedades catalíticas de esterasas y lipasas, debido a que pueden
Externí odkaz:
https://doaj.org/article/e71a7546c8a0451f8525df19a741f8e8
Autor:
Israel García-Cano, Diana Rocha-Mendoza, Amelia Farrés, Edith Ponce-Alquicira, Adriana Lopez-Arvizu
Publikováno v:
World Journal of Microbiology and Biotechnology. 37
The gene encoding N-acetylmuramoyl-L-alanine amidase in Latilactobacillus sakei isolated from a fermented meat product was cloned in two forms: its complete sequence (AmiC) and a truncated sequence without one of its anchoring LysM domains (AmiLysM4)
Autor:
Adriana López-Arvizu, Diana Rocha-Mendoza, Amelia Farrés, Edith Ponce-Alquicira, Israel García-Cano
Publikováno v:
World journal of microbiologybiotechnology. 37(11)
The gene encoding N-acetylmuramoyl-L-alanine amidase in Latilactobacillus sakei isolated from a fermented meat product was cloned in two forms: its complete sequence (AmiC) and without one of its anchoring LysM domains (AmiLysM4). Deletion of the Lys
Autor:
Silvia Moreno-Mendieta, Sergio Sánchez, Amelia Farrés, P. Aguilera, Romina Rodríguez-Sanoja, Daniel Guillen
Publikováno v:
Applied Microbiology and Biotechnology. 105:7551-7552
Autor:
Karen Manoutcharian, Zaira Sánchez-Cuapio, Sergio Sánchez, Silvia Armenta, Amelia Farrés, Romina Rodríguez-Sanoja, Alejandra Hernández-Santoyo
Publikováno v:
Data in Brief
Data in Brief, Vol 21, Iss, Pp 1944-1949 (2018)
Data in Brief, Vol 21, Iss, Pp 1944-1949 (2018)
Carbohydrate-binding modules (CBMs) are auxiliary domains into glycoside-hydrolases that allow the interaction between the insoluble substrate and the solubilized enzyme, through hydrophobic, CH-π interactions and hydrogen bonds. Here, we present th
Autor:
Jocelin Rizo, Romina Rodríguez-Sanoja, Daniel Guillen, Amelia Farrés, Gloria Díaz-Ruiz, Sergio Sánchez, Carmen Wacher
Publikováno v:
Critical reviews in food science and nutrition. 60(5)
For a long time, food microbiota has been studied using traditional microbiological techniques. With the arrival of molecular or culture-independent techniques, a strong understanding of microbiota dynamics has been achieved. However, analyzing the f
Autor:
Maribel Cayetano-Cruz, Marina Gutiérrez-Antón, Ara Itzel Pérez de los Santos, María Eugenia Hidalgo-Lara, Alejandro Santiago-Hernández, Amelia Farrés, Miguel Ángel Plascencia-Espinosa
Publikováno v:
Enzyme and Microbial Technology. 83:48-56
Zymomonas mobilis genes encoding INVA and INVB were expressed in Pichia pastoris, under the control of the strong AOX1 promoter, and the recombinant enzymes were named INVAAOX1 and INVBAOX1. The expression levels of INVAAOX1 (1660 U/mg) and INVBAOX1