Abstract

Sericin protein was extracted from silk using a water-based method. The impact of sericin on the aquatic environment and its behavior under various temperature conditions were thoroughly investigated. To assess the total protein content in the solutions derived from silk at different temperatures, the Lowry method was employed. Subsequently, sericin protein was isolated in its pure form. In order to gain deeper insights into the characteristics of sericin, both IR-spectrometric and UV-spectrometric analyses were conducted. These analyses provided valuable information about the molecular structure and properties of the sericin protein. Additionally, the study focused on determining the composition of amino acids present in the sericin protein. For this purpose, high-performance liquid chromatography (HPLC) was employed, allowing for precise quantification and identification of individual amino acids within the protein. Through these comprehensive analytical techniques and experiments, researchers aimed to unravel the properties, behavior, and potential applications of sericin protein, contributing to a better understanding of its role and impact in various environmental and temperature conditions.

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