Abstract:Keratin is widely recognized as a high-quality renewable protein resource for biomedical applications. A large amount of rabbit hair waste is produced in textile industries, because it has high medullary layer content, but poor spinnability. Therefore, it is of great significance to extract keratin from waste rabbit hair for recycling. In this research, an ultrasonic-assisted reducing agent-based extraction method was developed and applied to extract keratin from rabbit hair. The results showed that the ultras… Show more
“…Untreated wool (spectrum 1) records the following absorption bands: 3296 cm −1 (N-H and O-H), 2877 cm −1 (-CH 2 ), 1607 cm −1 (Amide I), 1527 cm −1 (Amide II), and 1244 cm −1 (Amide III). This information is close to that indicated in the literature [28][29][30]. The functionalization of the wool by protonation (spectrum 2) determines changes only at the level of the absorption bands of the free NH 2 groups that become + NH 3 (according to Equation (3)).…”
The beetroot peels can be a sustainable source of betalains that can dye the wool materials through green processes based on low water and energy consumption. Green chemistry in the extraction of betalains from colored food waste/peels from red beetroot involved the use of water as a solvent, without other additives. In order for the extract obtained to be able to dye the wool, it was necessary to functionalize betalains or even the wool. Three types of sustainable functionalizations were performed, with (1) acetic acid; (2) ethanol; and (3) arginine. For each functionalization, the mechanism that can justify dyeing the wool in intense colors was elucidated. The characterization of the extract was performed with the data provided by UV-VIS and HPLC-MS analyses. The characterization of the wool dyed with the extract obtained from the red beetroot peels was possible due to the information resulting from the FTIR and CIELab analyses. The functionalizations of betalains and wool in acid environments lead to the most intense red colors. The color varies depending on the pH and the concentration of betalains.
“…Untreated wool (spectrum 1) records the following absorption bands: 3296 cm −1 (N-H and O-H), 2877 cm −1 (-CH 2 ), 1607 cm −1 (Amide I), 1527 cm −1 (Amide II), and 1244 cm −1 (Amide III). This information is close to that indicated in the literature [28][29][30]. The functionalization of the wool by protonation (spectrum 2) determines changes only at the level of the absorption bands of the free NH 2 groups that become + NH 3 (according to Equation (3)).…”
The beetroot peels can be a sustainable source of betalains that can dye the wool materials through green processes based on low water and energy consumption. Green chemistry in the extraction of betalains from colored food waste/peels from red beetroot involved the use of water as a solvent, without other additives. In order for the extract obtained to be able to dye the wool, it was necessary to functionalize betalains or even the wool. Three types of sustainable functionalizations were performed, with (1) acetic acid; (2) ethanol; and (3) arginine. For each functionalization, the mechanism that can justify dyeing the wool in intense colors was elucidated. The characterization of the extract was performed with the data provided by UV-VIS and HPLC-MS analyses. The characterization of the wool dyed with the extract obtained from the red beetroot peels was possible due to the information resulting from the FTIR and CIELab analyses. The functionalizations of betalains and wool in acid environments lead to the most intense red colors. The color varies depending on the pH and the concentration of betalains.
“…The Shindai method was selected for the extraction of human hair keratin, as this method yields α- keratin and does not use any detergents [ 16 ]. The scaffold that was developed using a 1:3 and 1:4 ratio of keratin and PVA formed a continuous porous composite scaffold.…”
The aim of this study was to transform human hair keratin waste into a scaffold for soft tissue engineering to heal wounds. The keratin was extracted using the Shindai method. Keratin and polyvinyl alcohol (PVA) was cross-linked with alginate dialdehyde and converted into a scaffold by the freeze-drying method using gentamycin sulphate (GS) as a model drug. The scaffold was subjected to Fourier transform infrared spectra (FTIR), swelling index, porosity, water absorption, scanning electron microscopy (SEM), differential scanning calorimetry (DSC), thermal gravimetric analysis (TGA), X-ray diffraction (XRD), drug release, and cell viability (MTT) analysis. The scaffold was tested for keratinocyte growth using the murine fibroblast cell line (NIH 3T3 cells). The outcome from the keratin had a molecular weight band between 52–38 kDa in SDS-PAGE (Sodium dodecylsulfate-Polyacrylamide gel electrophoresis). A porous scaffold was capable of water absorption (73.64 ± 14.29%), swelling ability (68.93 ± 1.33%), and the release of GS shown as 97.45 ± 4.57 and 93.86 ± 5.22 of 1:4 and 1:3 scaffolds at 16 h. The physicochemical evaluation revealed that the prepared scaffold exhibits the proper structural integrity: partially crystalline with a strong thermal property. The scaffold demonstrated better cell viability against the murine fibroblast cell line (NIH 3T3 cells). In conclusion, we found that the prepared composite scaffold (1:4) can be used for wound healing applications.
“…The same tendency can be seen for ESPE with lower molecular weight compared to PRO and a slightly higher average particle size (293 nm compared to 334 nm) and lower zeta potential (−23.3 mV compared to –28.5 mV, respectively). The results showed that the performed hydrolyses were not as destructive for the keratin molecule as those reported for the enzymatic hydrolysates when the average particle size was reported to be 100–150 nm [ 36 ], but comparable to those of 750 nm, tested as a bioactive and biocompatible material for wound healing [ 34 ]. The self-assembling ability of keratin hydrolysate was also highlighted for keratin hydrolysates extracted by keratinase use [ 34 ] or by ultrasound assisted chemical extraction [ 37 ].…”
The aim of this paper was to select keratin hydrolysate with bioactive properties by using the enzymatic hydrolysis of wool. Different proteolytic enzymes such as Protamex, Esperase, and Valkerase were used to break keratin molecules in light of bioactive additive preparation. The enzymatic keratin hydrolysates were assessed in terms of the physico-chemical characteristics related to the content of dry substance, total nitrogen, keratin, ash, cysteic sulphur, and cysteine. The influence of enzymatic hydrolysis on molecular weight and amino acid composition was determined by gel permeation chromatography (GPC) and gas chromatography-mass spectrometry (GC-MS) analyses. Antimicrobial activity of keratin hydrolysates was analysed against Fusarium spp., a pathogenic fungus that can decrease the quality of plants. The bioactivity of enzymatic hydrolysates was tested on maize plants and allowed us to select the keratin hydrolysates processed with the Esperase and Valkerase enzymes. The ratio of organised structures of hydrolysate peptides was analysed by attenuated total reflectance-Fourier transform infrared (ATR-FTIR) deconvolution of the amide I band and may explain the difference in their bioactive behaviour. The most important modifications in the ATR spectra of maize leaves in correlation with the experimentally proven performance on maize development by plant length and chlorophyll index quantification were detailed. The potential of enzymatic hydrolysis to design additives with different bioactivity was shown in the case of plant growth stimulation.
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