Protease immobilization on cellulose monoacetate/chitosan-blended nanofibers

Autor: Tuba Avci, Elif Demirkan, Yakup Aykut
Přispěvatelé: Uludağ Üniversitesi/Fen-Edebiyat Fakültesi/Biyoloji Bölümü., Uludağ Üniversitesi/Mühendislik Fakültesi/Tekstil Mühendisliği Bölümü., Demirkan, Elif, Avcı, Tuba, Aykut, Yakup, ABI-4472-2020
Rok vydání: 2017
Předmět:
Glutaraldehyde activation
Polymers and Plastics
medicine.medical_treatment
Nanofibers
Chitin
02 engineering and technology
01 natural sciences
Differential scanning calorimeters
Industrial and Manufacturing Engineering
Physical adsorption method
Chitosan
chemistry.chemical_compound
Chemical Engineering (miscellaneous)
Chemical analysis
Enzyme activity
Catalysts
Fourier transform infrared spectroscopy
Spinning (fibers)
Cellulose acetates
Chemical activation
021001 nanoscience & nanotechnology
Microspheres
Electrospinning
Enzymes
Fibers
Thermogravimetric analyzers
0210 nano-technology
Scanning electron microscopy
Immobilized Enzymes
Candida Rugosa
Materials science
Immobilized enzyme
Cellulose acetate
Materials Science (miscellaneous)
Sodium
Immobilized enzyme activity
chemistry.chemical_element
010402 general chemistry
Sodium hydroxide
Differential scanning calorimetry
medicine
Enzyme immobilization
Cellulose
Membranes
Protease
Acetate
Alpha-amylase
Thermoanalysis
Lipase immobilization
Electrospinning process
0104 chemical sciences
chemistry
Chemical engineering
Nanofiber
Nanoparticles
Materials science
textiles
Zdroj: Journal of Industrial Textiles. 47:2092-2111
ISSN: 1530-8057
1528-0837
Popis: Chitosan-blended cellulose monoacetate nanofibers were prepared through electrospinning process. Neat nanofibers and their sodium hydroxide-treated analogs were used as support surfaces for protease immobilization via physical adsorption method. Morphologies of the nanofibers were observed with a scanning electron microscopy. Chemical analyses were conducted with Fourier transform infrared spectroscopy, and thermal analyses were carried out with differential scanning calorimeter and thermogravimetric analyzer. Immobilized enzyme activities were measured by using casein substrate. In order to test the stability of immobilized enzymes, the tests were repeated until the immobilized enzyme activity was leveled off. The results reveal that well uniform cellulose monoacetate/chitosan nanofibers were obtained, and nanofiber structures are transformed from rounded to more flattened morphology after enzyme activation test. Glutaraldehyde activation has positive effect on sodium hydroxide-treated samples, and the highest immobilization yield as about 83% was observed for glutaraldehyde-treated cellulose monoacetate/chitosan samples. Sodium hydroxide treatment before glutaraldehyde activation shows the best results for protease immobilization on cellulose monoacetate and cellulose monoacetate/chitosan nanofibers. Operational stability increases after sodium hydroxide treatment and glutaraldehyde activation. Glutaraldehyde activation effectively increased the cycle number after sodium hydroxide treatment and about 20% of enzyme activity was still retained after seven cycles at cellulose monoacetate/chitosan samples. This percentage is higher at pure cellulose monoacetate nanofibers than cellulose monoacetate/chitosan nanofibers and measured around 33.5%. British Association for Psychopharmacology Fırat Üniversitesi
Databáze: OpenAIRE