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A study of the role of calcium and oxidative stress in pathophysiology of osteoporosis in postmenopausal women-a review Haddig, Nour El-Houda; Zerzour, Aicha; Derouiche, Samir
JINAV: Journal of Information and Visualization Vol. 1 No. 2 (2020)
Publisher : Yayasan Ahmar Cendekia Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.35877/454RI.jinav255

Abstract

The aim of this review was to identify the role of calcium and oxidative stress as factors associated with osteoporosis in postmenopausal women. There are many diseases related to post-menstruation in women, the most important of which is osteoporosis. Calcium levels remains stable until menopause, when the bone resorption rate increases in association with the decrease in ovarian estrogen production that effect the intestinal calcium absorption. On the other hand, studies support that oxidative stress is directly involved in the genesis and development of osteoporosis. However, Oxidative stress blocks the activation of osteoblasts and activates the differentiation of osteoclasts which led to increased resorption rate without adequate and proper bone formation. In conclusion, Physiological changes in postmenopausal women lead to fluctuations in calcium metabolism and oxidative stress, which may lead to the occurrence or development of osteoporosis.
Comparative study of immobilized enzyme on nano-composite (SCN) and free enzyme of invertase isolated from baker's yeast Chouia, Maroua; Derouiche, Samir
Journal of Agriculture and Applied Biology Vol 6 No 2 (2025): Journal of Agriculture and Applied Biology
Publisher : Future Science

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.11594/jaab.06.02.09

Abstract

The objective of this study was to compare the properties and performance of invertase enzyme isolated from baker's yeast, both in free and immobilized form on a starch-copper nanocomposite (SCN). The SCN was synthesized using starch as a reducing agent for the biological production of copper nanoparticles (CuNPs). The Characterization of SCN was performed using Fourier transform infrared (FT-IR) spectroscopy, scanning electron microscopy (SEM), and X-ray diffraction to confirm nanoparticle formation and structural properties. The immobilization of invertase onto SCN was optimized by varying nanoparticle concentration, pH, incubation time, and temperature to maximize enzyme attachment and activity. Enzyme activity was measured for both free and immobilized forms to determine the immobilization efficiency. The study found that the high levels of enzyme immobilization were observed at pH = 9, temperature T = 30, and 3% SCN concentration. For both free and immobilized invertase, the ideal reaction temperatures were 35°C and 40°C, with corresponding pH values of 5 and 4.5. Reusability experiments revealed that the immobilized enzyme retained 49% of its activity after ten cycles, demonstrating improved stability and potential for repeated use. The results suggest that enzyme immobilization on SCN occurs through non-covalent interactions, providing a practical and sustainable approach for biocatalytic applications. This research highlights the potential of starch-based nanocomposites for enzyme stabilization, offering a cost-effective and environmentally friendly solution for industrial and biotechnological applications.
Comparative study of immobilized enzyme on nano-composite (SCN) and free enzyme of invertase isolated from baker's yeast Chouia, Maroua; Derouiche, Samir
Journal of Agriculture and Applied Biology Vol 6 No 2 (2025): Journal of Agriculture and Applied Biology
Publisher : Future Science

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.11594/jaab.06.02.09

Abstract

The objective of this study was to compare the properties and performance of invertase enzyme isolated from baker's yeast, both in free and immobilized form on a starch-copper nanocomposite (SCN). The SCN was synthesized using starch as a reducing agent for the biological production of copper nanoparticles (CuNPs). The Characterization of SCN was performed using Fourier transform infrared (FT-IR) spectroscopy, scanning electron microscopy (SEM), and X-ray diffraction to confirm nanoparticle formation and structural properties. The immobilization of invertase onto SCN was optimized by varying nanoparticle concentration, pH, incubation time, and temperature to maximize enzyme attachment and activity. Enzyme activity was measured for both free and immobilized forms to determine the immobilization efficiency. The study found that the high levels of enzyme immobilization were observed at pH = 9, temperature T = 30, and 3% SCN concentration. For both free and immobilized invertase, the ideal reaction temperatures were 35°C and 40°C, with corresponding pH values of 5 and 4.5. Reusability experiments revealed that the immobilized enzyme retained 49% of its activity after ten cycles, demonstrating improved stability and potential for repeated use. The results suggest that enzyme immobilization on SCN occurs through non-covalent interactions, providing a practical and sustainable approach for biocatalytic applications. This research highlights the potential of starch-based nanocomposites for enzyme stabilization, offering a cost-effective and environmentally friendly solution for industrial and biotechnological applications.