?-Amylase Immobilization on P(HEMA-co-PEGMA) Hydrogels: Preparation, Characterization, and Catalytic Investigation
dc.authorid | Ateş, Burhan/0000-0001-6080-229X | |
dc.authorid | Ulu, Ahmet/0000-0002-4447-6233 | |
dc.authorwosid | Ateş, Burhan/AAA-3730-2021 | |
dc.authorwosid | Ulu, Ahmet/L-5180-2016 | |
dc.contributor.author | Dogan, Demet | |
dc.contributor.author | Ulu, Ahmet | |
dc.contributor.author | Sel, Evren | |
dc.contributor.author | Koytepe, Suleyman | |
dc.contributor.author | Ates, Burhan | |
dc.date.accessioned | 2024-08-04T20:50:14Z | |
dc.date.available | 2024-08-04T20:50:14Z | |
dc.date.issued | 2021 | |
dc.department | İnönü Üniversitesi | en_US |
dc.description.abstract | The aims of this study are to synthesize and characterize poly (2-hydroxyethyl methacrylate-co-poly (ethylene glycol) methacrylate) (P(HEMA-co-PEG500MA)) structures containing polyethylene glycol (PEG) side groups and to investigate their possible use in alpha-amylase immobilization. For this purpose, P(HEMA-co-PEG500MA) copolymer structures are synthesized by using different monomer ratios. P(HEMA-co-PEG500MA) copolymer structures are confirmed by Fourier transform infrared spectroscopy (FTIR), and elemental analysis techniques. In addition, thermal, and morphological properties of the copolymers are investigated by thermal gravimetric analysis/differential scanning calorimetry, and scanning electron microscopy (SEM). Afterward, alpha-amylase from Aspergillus oryzae is immobilized on synthesized copolymer support by using physical interactions. The success of immobilization is elucidated via FTIR, SEM, and energy dispersive X-ray spectroscopy (EDX) methods. In addition, the influences of temperature, pH, storage time, and repeated uses on the activity of free and immobilized alpha-amylase are investigated. According to the outcomes, the immobilized alpha-amylase possesses a better pH and thermal resistance than the free one. Additionally, the immobilized alpha-amylase maintains about 53% of its original activity after eight reuses and it exhibits about 50% relative activity after 28 days of storage. In conclusion, the immobilized alpha-amylase can be utilized as a potential efficient catalyst to produce maltose from the hydrolysis of starch. | en_US |
dc.identifier.doi | 10.1002/star.202000217 | |
dc.identifier.issn | 0038-9056 | |
dc.identifier.issn | 1521-379X | |
dc.identifier.issue | 7-8 | en_US |
dc.identifier.scopus | 2-s2.0-85105943076 | en_US |
dc.identifier.scopusquality | Q2 | en_US |
dc.identifier.uri | https://doi.org/10.1002/star.202000217 | |
dc.identifier.uri | https://hdl.handle.net/11616/99928 | |
dc.identifier.volume | 73 | en_US |
dc.identifier.wos | WOS:000651011700001 | en_US |
dc.identifier.wosquality | Q3 | en_US |
dc.indekslendigikaynak | Web of Science | en_US |
dc.indekslendigikaynak | Scopus | en_US |
dc.language.iso | en | en_US |
dc.publisher | Wiley-V C H Verlag Gmbh | en_US |
dc.relation.ispartof | Starch-Starke | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | copolymer s | en_US |
dc.subject | enzyme immobilization | en_US |
dc.subject | improved stability | en_US |
dc.subject | starch hydrolysis | en_US |
dc.subject | ? ? amylase | en_US |
dc.title | ?-Amylase Immobilization on P(HEMA-co-PEGMA) Hydrogels: Preparation, Characterization, and Catalytic Investigation | en_US |
dc.type | Article | en_US |