Development and characterization of antioxidant and antimicrobial edible films based on chitosan and gamma-aminobutyric acid-rich fermented soy protein

2020 ◽  
Vol 244 ◽  
pp. 116491 ◽  
Author(s):  
Zahra Zareie ◽  
Farideh Tabatabaei Yazdi ◽  
Seyed Ali Mortazavi
Keyword(s):  
Soy Protein ◽  
Edible Films ◽  
Aminobutyric Acid ◽  
Gamma Aminobutyric Acid

scholarly journals Development and characterization of a novel soy protein isolate based composite film enriched with glycyrrhizin nanogel particles.

2021 ◽  
Author(s):  
Aritra Sinha
Keyword(s):  
Antioxidant Activity ◽  
Water Vapor ◽  
Soy Protein ◽  
Soy Protein Isolate ◽  
Water Vapor Permeability ◽  
Edible Films ◽  
Protein Isolate ◽  
Vapor Permeability ◽  
Barrier Performance

Abstract This study focuses on the development and characterization of a novel biodegradable edible film made from soy protein isolate enriched with alginate-glycyrrhizin nanogel(GL-ALG NGP). Nanoparticles of particle sizes below 100 nm were synthesized using glycyrrhizin(GL), calcium chloride and, sodium alginate(SA) through the reverse micro-emulsion/internal gelation method. Soy protein isolate (SPI) based films were prepared by a simple casting procedure by incorporating GL-ALG NGPs in SPI solution in different ratios of (SPI: GL-ALG NGPs) 5:0, 5:1, 2:1, 1:1, and 1:1.5. Glycerol was used as a plasticizer in the film-forming solution. The effects of the proportions of GL-ALG NGPs addition on the thickness, mechanical properties, water vapor permeability, UV barrier performance, antioxidant activity, and antimicrobial property of the obtained films were studied. The GL-ALG NGPs were analyzed using Dynamic Light Scattering. Microstructural studies of obtained films were performed using Scanning Electron microscopy. Results show incorporation of GL-ALG NGPs in soy protein-alginate complex produced smoother, compact, and more continuous matrices as compared to pure SPI films. The test results indicated that blending of SPI with GL-ALG NGPs in the ratio 1:1 increased tensile strength of obtained films by 185%, reduced water solubility to 23.59%, and water vapor permeability to 0.3087 g-mm/m2-d-kPa. Obtained films exhibited good UV barrier performance, antioxidant activity and inhibited the growth of E. coli, S. aureus, Enterobacter sakazakii, and A. niger. So, soy protein isolate-based films enriched with GL-ALG NGPs are active biodegradable edible films that can be used to extend the shelf life of food products.

scholarly journals Search for Structural Basis of Interactions of Biogenic Amines with Human TAAR1 and TAAR6 Receptors

2021 ◽  
Vol 23 (1) ◽  
pp. 209
Author(s):  
Anna V. Glyakina ◽  
Constantine D. Pavlov ◽  
Julia V. Sopova ◽  
Raul R. Gainetdinov ◽  
Elena I. Leonova ◽  
...  
Keyword(s):  
Biogenic Amines ◽  
Binding Sites ◽  
Aminobutyric Acid ◽  
Structural Basis ◽  
Gamma Aminobutyric Acid ◽  
Class A ◽  
Trace Amine ◽  
First Time ◽  
Identification And Characterization

The identification and characterization of ligand-receptor binding sites are important for drug development. Trace amine-associated receptors (TAARs, members of the class A GPCR family) can interact with different biogenic amines and their metabolites, but the structural basis for their recognition by the TAARs is not well understood. In this work, we have revealed for the first time a group of conserved motifs (fingerprints) characterizing TAARs and studied the docking of aromatic (β-phenylethylamine, tyramine) and aliphatic (putrescine and cadaverine) ligands, including gamma-aminobutyric acid, with human TAAR1 and TAAR6 receptors. We have identified orthosteric binding sites for TAAR1 (Asp68, Asp102, Asp284) and TAAR6 (Asp78, Asp112, Asp202). By analyzing the binding results of 7500 structures, we determined that putrescine and cadaverine bind to TAAR1 at one site, Asp68 + Asp102, and to TAAR6 at two sites, Asp78 + Asp112 and Asp112 + Asp202. Tyramine binds to TAAR6 at the same two sites as putrescine and cadaverine and does not bind to TAAR1 at the selected Asp residues. β-Phenylethylamine and gamma-aminobutyric acid do not bind to the TAAR1 and TAAR6 receptors at the selected Asp residues. The search for ligands targeting allosteric and orthosteric sites of TAARs has excellent pharmaceutical potential.

scholarly journals Characterization of the phenotype and birthdates of pyknotic dead cells in the nervous system by a combination of DNA staining and immunohistochemistry for 5'-bromodeoxyuridine and neural antigens.

1993 ◽  
Vol 41 (6) ◽  
pp. 819-827 ◽  
Author(s):  
E Soriano ◽  
J A Del Río ◽  
C Auladell
Keyword(s):  
Nervous System ◽  
Normal Development ◽  
Temporal Distribution ◽  
Neural Tissue ◽  
Aminobutyric Acid ◽  
Phenotypic Characterization ◽  
Gamma Aminobutyric Acid ◽  
Pregnant Mice ◽  
The Times

Cells displaying highly condensed pyknotic nuclei, the most characteristic feature of apoptosis, are considered as dead cells in neural tissue. The present study aimed to devise methods that could allow the neurogenetic and phenotypic characterization of dying pyknotic cells. In the first set of experiments, pregnant mice were labeled at embryonic days E10-E16 with pulses of 5'-bromodeoxyuridine visualization of BrdU after an immunoperoxidase reaction. In addition to normal, healthy immunopositive nuclei, these preparations displayed a number of pyknotic nuclei that were immunoreactive for BrdU. Both the regional and the temporal distribution of BrdU-positive pyknotic cells were coincidental with the peaks of dead cells in neural tissue. For example, pulses of BrdU at E10-E11 resulted in the visualization of immunoreactive pyknotic cells in the subplate and white matter of the cerebral cortex in early postnatal (P) animals. Thus, the times of generation (birthdates) of cells subjected to degenerative processes can be unequivocally identified. In the second set of experiments, brain sections from unlabeled littermates were immunostained for a variety of neural and glial markers and counterstained with bisbenzimide, to find antigens which, by being present in degenerate pyknotic cells, could indicate the phenotype of such cells. Although no pyknotic cells were positively immunostained for neurofilaments, neuropeptide Y, somatostatin, vasoactive intestinal polypeptide, or vimentin, a number of pyknotic cells were found to be immunoreactive for microtubule-associated protein 2, gamma-aminobutyric acid, calbindin 28KD, and glial fibrillary acidic protein. The percentage of pyknotic cells labeled with neural antigens accounted for more than 20% of the total number of pyknotic cells in a given brain region. In contrast, GFAP-positive pyknotic cells represented up to 50% of the total pyknotic cell population. The method shown here has enabled us to determine that both neurons and glial cells undergo degeneration during normal development.

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