A5079444408- Enzyme Catalysis and Immobilization
- Catalysis for Biomass Conversion
- Enzyme Production and Characterization
- Biofuel production and bioconversion
- Microbial Metabolites in Food Biotechnology
- Electrochemical sensors and biosensors
- Optical properties and cooling technologies in crystalline materials
- Amino Acid Enzymes and Metabolism
- Microbial Metabolic Engineering and Bioproduction
- Perovskite Materials and Applications
- Enzyme Structure and Function
- Luminescence Properties of Advanced Materials
Cukurova University
2021-2025
This study presents that covalent immobilization technique has been utilized for the of l-lactate dehydrogenase (l-LDH) from porcine on mesoporous silica. To develop silica as support material use in l-LDH immobilization, particle surfaces were functionalized with 3-aminopropyltrimethoxysilane and further conjugated glutaraldehyde. The effect some parameters such glutaraldehyde concentration, pH, initial enzyme time was investigated optimum conditions these determined 1% (w/v), pH 8.0, 1...
<title>Abstract</title> In this study, Fe<sub>3</sub>O<sub>4</sub>-coated multi-walled carbon nanotubes (MWCNT-Fe<sub>3</sub>O<sub>4</sub>) or nickel oxide-coated (MWCNT-NiO) were activated with 3-glycidyloxypropyl)trimethoxysilane to create oxirane groups. Pullulanase from <italic>Bacillus licheniformis</italic> was covalently immobilized on these magnetic MWCNTs obtain magnetically separable pullunase preparations (MWCNT-Fe<sub>3</sub>O<sub>4</sub>@Pul MWCNT-NiO@Pul) for producing...
Abstract Magnetic nickel oxide multi‐walled carbon nanotubes (MWCNT‐NiO) were employed in the immobilization of xylanase from Thermomyces lanuginosus , after modification with (3‐glycidoxypropyl)trimethoxysilane or 3‐aminopropyltriethoxysilane (APTES). The APTES‐derivatized MWCNT‐NiO particles activated glutaraldehyde to immobilize T. via covalent attachment. (3‐glycidoxypropyl)trimethoxysilane‐derivatized directly used for xylanase, formed epoxy groups converted aldehyde groups. free had...