This study aims to research and analyze a newly identified plant-based protease for potential applications within the cosmetic industry. The research focuses on isolating and characterizing a protease enzyme derived from Freesia refracta flowers. The purification method involves employing ammonium sulfate precipitation and ion exchange chromatography. Additionally, the protease's substrate specificity will beexamined, particularly its reactions with azoalbumin and serum albumin.Enzymatic kinetics, inclusive of determining Vmax and Km values using Lineweaver-Burk plots, yielded readings of 0.784 mg/L.min and 0.317 mM, respectively. Furthermore, SDS-PAGE and gel filtration chromatography were utilized to determine the enzyme's degree of purification and molecular weight, indicating a molecular weight of 24 kDa. These outcomes identify the specific protease obtained from Freesia flowers, suggesting its potential suitability for cosmetic applications.Moreover, investigations into the impact of various compounds SDS, DIPF, EDTA, phenanthraline, iodoacetamide, Ca2+, Zn2+, Hg2+, and Co2+at a 10 mM concentration significantly enhanced the enzymatic activity of the purified protease. The research findings affirm the successful utilization of the protease extracted from Freesia flowers (Freesia refracta) in cosmetic formulations, showcasing its practical suitability for cosmetic production.
Primary Language | English |
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Subjects | Medical Biotechnology (Other), Micro and Nanosystems |
Journal Section | Research Articles |
Authors | |
Publication Date | December 15, 2023 |
Submission Date | October 10, 2023 |
Acceptance Date | December 10, 2023 |
Published in Issue | Year 2023 Volume: 7 Issue: 2 |