Chemical Engineering / Kimya Mühendisliği
Permanent URI for this collectionhttps://hdl.handle.net/11147/14
Browse
2 results
Search Results
Article Citation - WoS: 5Citation - Scopus: 5Novel Biopolymer-Based Hydrogels Obtained Through Crosslinking of Keratose Proteins Using Tetrakis(hydroxymethyl) Phosphonium Chloride(Springer, 2022) Yalçın, Damla; Top, AybenMerino wool obtained from the Karacabey region of Turkey was solubilized using peracetic acid oxidation. The wool and extracted wool proteins (keratose) were characterized using SEM, XRD, TGA, and FTIR analyses. SDS-PAGE result of the keratose indicated diffusive bands were populated between ~ 40 and ~ 55 kDa, corresponding to low-sulfur content α-keratose proteins. Chemically crosslinked hydrogels were prepared using the keratose and tetrakis(hydroxymethyl) phosphonium chloride (THPC). Storage moduli of the hydrogels prepared at 1:1, 1:2, and 1:4 keratose to THPC reactive group ratios were measured as 63 ± 22, 291 ± 21, and 804 ± 53 Pa, respectively. Crosslinking degrees of the hydrogels also affected the secondary structures of the keratose films obtained from the drying of the hydrogels. The hydrogel with the highest crosslinking density (1:4 gel) exhibited the lowest swelling ratio, whereas the one with the lowest crosslinking density (1:1 gel) disintegrated in deionized water within less than 6 h. CCK-8 tests using L929 mouse fibroblast cells showed that all the hydrogels promoted cell proliferation. These results suggest THPC crosslinked hydrogels prepared at the millimolar THPC concentrations are biocompatible scaffolds, which can be utilized in drug delivery and tissue engineering applications. Graphical abstract: [Figure not available: see fulltext.]Article Citation - WoS: 24Citation - Scopus: 26Self-Assembly Behavior of the Keratose Proteins Extracted From Oxidized Ovis Aries Wool Fibers(Elsevier Ltd., 2019) Pakkaner, Efecan; Yalçın, Damla; Uysal, Berk; Top, AybenWater soluble keratose proteins were obtained from an Ovis Aries wool using peracetic acid oxidation. The wool samples and the extracted keratose proteins were characterized by using FTIR, XRD, SEM and TGA techniques. Fractions of alpha-keratose (MW = 43-53 kDa) along with protein species with molecular weights between 23 kDa and 33 kDa were identified in the SDS-PAGE analysis result of the extracted protein mixture. DLS and AFM experiments indicated that self-assembled globular nanoparticles with diameters between 15 nm and 100 nm formed at 5 mg/ml keratose concentration. On the other hand, upon incubation of 10 w % keratose solutions at 37 degrees C and 50 degrees C, interconnected keratose hydrogels with respective storage modulus (G') values of 0.17 +/- 0.03 kPa and 3.7 +/- 0.5 kPa were obtained. It was shown that the keratose hydrogel prepared at 37 degrees C supported L929 mouse fibroblast cell proliferation which suggested that these keratose hydrogels could be promising candidates in soft tissue engineering applications. (C) 2018 Elsevier B.V. All rights reserved.