Volume 11, Issue 41 (11-2020)                   NCMBJ 2020, 11(41): 29-46 | Back to browse issues page

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Saleknezhad M. Increasing the stability of keratin protein solubility in aqueous solutions using the chemical structure modification by alkylation and sulfitolysis methods. NCMBJ 2020; 11 (41) :29-46
URL: http://ncmbjpiau.ir/article-1-1333-en.html
Abstract:   (2208 Views)
Aim and Background:In the past two decades, proteins and peptides have become an important class of therapeutic drugs. However, their sensitivity to chemical and physical degradation has posed challenges for scientists. Approximate 90% of the chicken feather of slaughterhouse waste is Keratin. Keratin protein is insoluble in water and has a strong tendency to accumulate and precipitate. Today, the stability of proteins in pharmaceutical applications is of great importance.
Materials and Methods:In this study, Keratin was extracted from feather by sodium hydroxide 0.2 M and hydrolyzed by 8% (V/V) Alcalase enzyme in 55 Celsius, at 8 pH. The hydrolyzed Keratin solution was chemically modified by alkylation and sulfitolysis to reduce aggregation. Keratin solubility, degree of chemical modification, percentage of stability, mol amount of free thiol, also DLS, and FTIR of the samples were investigated.
The result showed that the degree of chemical modification of Keratin in the alkylation method was 72% and the sulfitolysis method was 66%. The chemical modification of hydrolyzed Keratin was reduced aggregation at pH3 to 288.65% and 335.3% for alkylation method and sulfitolysis respectively. Investigation of the stability and preservation of protein content showed that the stability of modified Keratin by alkylation method was 81.9% and by sulfitolysis method was 86.3% in 30 days, but the hydrolyzed Keratin as a control preserved only 9.8% of protein content. The result of the DLS test shows that the Keratin modified by alkylation in water has PI=0.476 and a mean particle size of 157.3 nm and Keratin modified by sulfitolysis in water has PI=0.475 and a mean particle size of 136.2 nm, which was more uniform and dispersed than the hydrolyzed Keratin with PI=0.552 and a mean particle size of 990.3 nm.
Conclusion:The chemical modification of hydrolyzed Keratin was a permanent change and binding of expected groups increased the Keratin solubility in aqueous solution and decreases the aggregation at acidic pH. The results of the FTIR analysis confirmed the chemical modification of Keratin.
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Type of Study: Research Article | Subject: Cellular and molecular
Received: 2020/12/20 | Accepted: 2020/11/30 | Published: 2020/11/30

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