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, often hailed as a holistic "health package", comprises an array of nutritional components and active compounds, contributing to its esteemed status in the realm of healthy foods. In this study, a comprehensive analysis was performed to elucidate the diverse nutritional profiles, bioactive components, and antiproliferative activities between two species: (GLU) and (GLE). The results showed that GLE possessed a higher level of nutritional constituents, except for dietary fiber. Fatty acid analysis revealed comparable profiles rich in unsaturated fatty acids for both species. The ethanol extract of GLU and GLE exhibited potent antioxidant capabilities and remarkable inhibition of tumor cell proliferation via apoptosis induction, with greater potency in GLE. The heightened triterpene levels in GLE potentially contribute to its augmented antitumoral effects. The exploration emphasized the significance of comprehending the varied chemical compositions of species, providing insights into their potential health benefits applications in the food and pharmaceutical industries.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10888466 | PMC |
http://dx.doi.org/10.3390/foods13040614 | DOI Listing |
Foods
February 2024
Biotechnology and Nuclear Technology Research Institute, Sichuan Academy of Agricultural Sciences, Chengdu 610061, China.
, often hailed as a holistic "health package", comprises an array of nutritional components and active compounds, contributing to its esteemed status in the realm of healthy foods. In this study, a comprehensive analysis was performed to elucidate the diverse nutritional profiles, bioactive components, and antiproliferative activities between two species: (GLU) and (GLE). The results showed that GLE possessed a higher level of nutritional constituents, except for dietary fiber.
View Article and Find Full Text PDFBiochemistry
February 2011
Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Navy Nagar, Colaba, Mumbai 400 005, India.
The molecular basis of the post-translational modification involving covalent attachment of the heme with a glutamic acid observed in some enzymes of the CYP4 family of heme monooxygenases has been investigated using site-directed mutagenesis of CYP175A1 from Thermus thermophilus. Earlier studies of CYP4 as well as the G248E mutant of CYP101A1 showed covalent linkage of the heme to a conserved glutamic acid of helix I. We have introduced Glu/Asp at the Leu80 position in the β-turn of CYP175A1, on the basis of molecular modeling studies, to assess whether formation of such a covalent linkage is limited only to helix I or whether such modification may also take place with the residue that is spatially located at a position appropriate for activation by the heme peroxidase reaction.
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