Please use this identifier to cite or link to this item: http://hdl.handle.net/11452/31077
Title: Cellulose monoacetate/polycaprolactone and cellulose monoacetate/polycaprolactam blended nanofibers for protease immobilization
Authors: Uludağ Üniversitesi/Mühendislik Fakültesi/Tekstil Mühendisliği Bölümü.
Uludağ Üniversitesi/Fen-Edebiyat Fakültesi/Biyoloji Bölümü.
0000-0002-7528-9529
Aykut, Yakup
Sevgi, Tuba
Demirkan, Elif
ABI-4472-2020
AAG-7112-2021
55320835000
57191880859
23469245200
Keywords: Polymer science
Cellulose and other wood products
Fibers
Textiles
Thermoplastics
Nanostructured polymers
Pa6 dispersed phase
Enzyme immobilization
Biomimetic mineralization
Selective localization
Morphology evolution
Acetate nanofibers
Carbon nanotubes
Ultrafine fibers
PP/pa6 blends
Electrospun
Cellulose
Thermoplastics
Wood Products
Polymers
Enzymes
Fibers
Nanofibers
Reusability
Textiles
Thermoplastics
Wood
Electrospinning process
Immobilized enzyme
Immobilized enzyme activity
Nanostructured polymers
Physical adsorption method
Polycaprolactam
Protease enzyme
Supporting surfaces
Enzyme activity
Issue Date: 25-Jun-2017
Publisher: Wiley
Citation: Aykut, Y. vd. (2017). ''Cellulose monoacetate/polycaprolactone and cellulose monoacetate/polycaprolactam blended nanofibers for protease immobilization''. Journal of Applied Polymer Science, 134(44).
Abstract: Enzymes can be used multiple times when they are immobilized on a support. More enzymes can be immobilized on a surface when nanofibers are used as a supporting surface because the specific surface area increases tremendously. In this regard, polycaprolactam/cellulose monoacetate (PA6/CMA) and polycaprolactone/cellulose monoacetate (PCL/CMA) blended nanofibers (NFs) were prepared via an electrospinning process. Protease enzymes were immobilized on neat PA6, PCL, PA6/CMA, and PCL/CMA nanofibers and glutaraldehyde (GA) activated analogs through the physical adsorption method. The immobilized enzyme activity was measured by using a casein substrate, and the results were compared with free enzyme activity. Among all of the samples, the highest immobilization yield of about 82% was obtained with GA-activated neat PCL NF samples. The best remaining activity of the immobilized enzymes on pure CMA NFs was found to be 59% after seven reuses. Even after nine reuses, enzyme activities are still observed on the CMA NF samples. It was expected that the addition of CMA in PCL and PA6 NFs would increase the reusability number to reach the reusability of CMA NFs, but it was not significantly enhanced. If CMA chains could be mostly collected on the sheath or close to the sheath of the NFs during the electrospinnig process, this target could be achieved.
URI: https://doi.org/10.1002/app.45479
https://onlinelibrary.wiley.com/doi/10.1002/app.45479
http://hdl.handle.net/11452/31077
ISSN: 0021-8995
1097-4628
Appears in Collections:Scopus
Web of Science

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