Autor: |
Škerget M; Laboratory for Separation Processes and Product Design, Faculty of Chemistry and Chemical Engineering, University of Maribor, Smetanova 17, 2000 Maribor, Slovenia., Čolnik M; Laboratory for Separation Processes and Product Design, Faculty of Chemistry and Chemical Engineering, University of Maribor, Smetanova 17, 2000 Maribor, Slovenia., Zemljič LF; Laboratory for Characterization and Processing of Polymers, Faculty of Mechanical Engineering, University of Maribor, Smetanova 17, 2000 Maribor, Slovenia., Gradišnik L; Institute of Biomedical Sciences, Faculty of Medicine, University of Maribor, Taborska 8, 2000 Maribor, Slovenia., Semren TŽ; Analytical Toxicology and Mineral Metabolism Unit, Institute for Medical Research and Occupational Health, Ksaverska Cesta 2, 10000 Zagreb, Croatia., Lovaković BT; Analytical Toxicology and Mineral Metabolism Unit, Institute for Medical Research and Occupational Health, Ksaverska Cesta 2, 10000 Zagreb, Croatia., Maver U; Institute of Biomedical Sciences, Faculty of Medicine, University of Maribor, Taborska 8, 2000 Maribor, Slovenia.; Department of Pharmacology, Faculty of Medicine, University of Maribor, Taborska 8, 2000 Maribor, Slovenia. |
Abstrakt: |
The isolation of keratin from poultry feathers using subcritical water was studied in a batch reactor at temperatures (120-250 °C) and reaction times (5-75 min). The hydrolyzed product was characterized by FTIR and elemental analysis, while the molecular weight of the isolated product was determined by SDS-PAGE electrophoresis. To determine whether disulfide bond cleavage was followed by depolymerization of protein molecules to amino acids, the concentration of 27 amino acids in the hydrolysate was analyzed by GC/MS. The optimal operating parameters for obtaining a high molecular weight protein hydrolysate from poultry feathers were 180 °C and 60 min. The molecular weight of the protein hydrolysate obtained under optimal conditions ranged from 4.5 to 12 kDa, and the content of amino acids in the dried product was low (2.53% w / w ). Elemental and FTIR analyses of unprocessed feathers and dried hydrolysate obtained under optimal conditions showed no significant differences in protein content and structure. Obtained hydrolysate is a colloidal solution with a tendency for particle agglomeration. Finally, a positive influence on skin fibroblast viability was observed for the hydrolysate obtained under optimal processing conditions for concentrations below 6.25 mg/mL, which makes the product interesting for various biomedical applications. |