Cargando…
Entrapment of α-Amylase in Agar Beads for Biocatalysis of Macromolecular Substrate
Attempts have been made to optimize immobilization parameters, catalytic property, and stability of immobilized α-amylase in agar. The work compares natural entrapment efficiency of agar with the ionotropically cross-linked agar hydrogel, with the advantage of easy scale-up and cost and time effecti...
Autores principales: | Sharma, Manu, Sharma, Vinay, Majumdar, Dipak K. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4897204/ https://www.ncbi.nlm.nih.gov/pubmed/27382608 http://dx.doi.org/10.1155/2014/936129 |
Ejemplares similares
-
Macromolecular Crowding Enhances Catalytic Efficiency and Stability of α-Amylase
por: Yadav, Jay Kant
Publicado: (2012) -
Influence of Tableting on Enzymatic Activity of Papain along with Determination of Its Percolation Threshold with Microcrystalline Cellulose
por: Sharma, Manu, et al.
Publicado: (2014) -
Improvement of Starch Digestion Using α-Amylase Entrapped in Pectin-Polyvinyl Alcohol Blend
por: Cruz, Maurício, et al.
Publicado: (2015) -
Polymer-Assisted Biocatalysis: Effects of Macromolecular
Architectures on the Stability and Catalytic Activity of Immobilized
Enzymes toward Water-Soluble and Water-Insoluble Substrates
por: Scheibel, Dieter M., et al.
Publicado: (2018) -
Development of enteric submicron particle formulation of papain for oral delivery
por: Sharma, Manu, et al.
Publicado: (2011)