Cellulose monoacetate/polycaprolactone and cellulose monoacetate/polycaprolactam blended nanofibers for protease immobilization

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. © 2017 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2017, 134, 45479.

Robust biodegradation of naproxen and diclofenac by laccase immobilized using electrospun nanofibers with enhanced stability and reusability

“…A wide range of polymers are used to enzyme immobilization, and poly(ε-caprolactone) [16] and poly(vinyl alcohol) are one of them [17]. It is worth to paying attention that during the production of electrospun nanofibers it is possible to obtain composite which, having many functional groups, increase the affinity of the enzyme to the support, for example polycaprolactone/cellulose monoacetate [18] and poly(vinyl alcohol)/polyacrylamide [19].…”

IMMOBILIZATION OF Bacillus subtilis E6-5 PROTEASE AND COMMERCIAL PROTEASE IN NANOFIBRILS CONTAINING DIFFERENT AMINO ACIDS

“…Enzymes immobilized PA/Tyrosine/GA NFs were considered to be the most successful immobilization, with maintaining 43 % of their activity up to 4 repetitions. Aykut et al (2017) prepared cellulose monoacetate/polycaprolactone and cellulose monoacetate/ polycaprolactamand activated the surfaces with aldehyde groups for protease immobilization. They obtained 35.5 % efficiency after eight reuses, and enzyme activities of about 23 % were still observed even after nine reuses (both for GA-activated and inactivated, pure CMA NF samples).…”

Enzyme immobilization: polymer–solvent–enzyme compatibility

“…Most of the reported co-immobilized enzymes were produced by entrapment and encapsulation in polymer matrices. For example, water-in-oil microemulsion encapsulation was performed using polycaprolactone (PCL) and its copolymers, 142 polylactic acid (PLA), 171 and poly(lactide- co -glycolide) (PLGA), 172 while entrapment was accomplished through in situ polymerization of polyacrylamide with enzymes in the reaction mixture. 124 However, some physically adsorbed co-immobilized enzymes were also reported.…”

“…141 Blending polymers or making copolymers is another way of enhancing enzyme affinity through the introduction of chemically functional side groups and polarity. Commonly used copolymer and polymer blends are cellulose acetate/ PCL, 142 cellulose acetate/polyamide, 143 chitosan/PVA, 144 chitosan/PLA, 145 PMMA/PANi, 146 polyvinyl alcohol-polyvinyl acrylic acid (PVA-PAA), 82 PVA-PEG, 147 methacrylate-gpoly(ethylene terephthalate)), 85 poly (vinyl alcohol-coethylene), 33 and poly(N-isopropyl acrylamide-co-acrylic acid). 11 Table 2 lists polymer-enzyme combinations that are immobilized through the post-immobilization process, where enzymes are attached to prefabricated carrier materials.…”