Cargando…
Cohnella amylopullulanases: Biochemical characterization of two recombinant thermophilic enzymes
Some industries require newer, more efficient recombinant enzymes to accelerate their ongoing biochemical reactions in harsh environments with less replenishment. Thus, the search for native enzymes from extremophiles that are suitable for use under industrial conditions is a permanent challenge for...
Autores principales: | Zebardast Roodi, Fatemeh, Aminzadeh, Saeed, Farrokhi, Naser, Karkhane, AliAsghar, Haghbeen, Kamahldin |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5386253/ https://www.ncbi.nlm.nih.gov/pubmed/28394913 http://dx.doi.org/10.1371/journal.pone.0175013 |
Ejemplares similares
-
Thermostable chitinase from Cohnella sp. A01: isolation and product optimization
por: Aliabadi, Nasrin, et al.
Publicado: (2016) -
Cohnella sp. A01 laccase: thermostable, detergent resistant, anti-environmental and industrial pollutants enzyme
por: Shafiei, Masoomeh, et al.
Publicado: (2019) -
Expression, characterization, and activity optimization of a novel cellulase from the thermophilic bacteria Cohnella sp. A01
por: Mohammadi, Shima, et al.
Publicado: (2022) -
Biochemical Characterization of Recombinant Thermostable Cohnella sp. A01 β-Glucanase
por: Rezaie, Meysam, et al.
Publicado: (2018) -
Cloning and expression of Saccharomyces cerevisiae SUC2 gene in yeast platform and characterization of recombinant enzyme biochemical properties
por: Mohandesi, Nooshin, et al.
Publicado: (2016)