Lutein and the Underlying Neuroprotective Promise against Neurodegenerative Diseases.

Alzheimer's disease (AD) and Parkinson's diseases (PD) are the two most common progressive neurodegenerative diseases with limited knowledge on their cause and, presently, have no cure. There is an existence of multiple treatment methods that target only the symptoms temporarily and do not stop the progression or prevent the onset of disease. Neurodegeneration is primarily attributed to the natural process of aging and the deleterious effects of heightened oxidative stress within the brain, whether via direct or indirect mechanisms. Emerging evidence suggests that certain nutritional aspects play a crucial role in the prevention and management of neurodegenerative diseases. Lutein, a dietary carotenoid, has been studied for its antioxidant properties for more than a decade with several applications against age-related macular degeneration. It is high antioxidant potential and selective accumulation in the brain makes it a versatile compound for combatting various neurodegenerative diseases. In this review, the studies exhibiting neuroprotective properties of lutein against neurodegenerative conditions, more specifically AD and PD in various model systems as well as clinical observations have been reviewed. Accordingly, the concerns associated with lutein absorption and potential strategies to improve its bioavailability have been discussed.

Oxidative stability of lutein on exposure to varied extrinsic factors.

Pre-processing treatments performed on lutein sources can cause it to degrade, generating superfluous metabolites and lowering lutein's bioactivity. However, evidences suggesting extent of reduction in functional stability of lutein on exposure to such treatment conditions are nil. This study is first of its kind, where we attempted to gain clarity on the extent of degradation caused by the changes in temperature (40-100 °C), pH (2-8) and duration of such treatments. Increase (3.9 folds) in lutein loss within an hour at 40 °C occurred when pH was lowered from 8 to 2. Increase (1.7 folds) in lutein loss at neutral pH and 40 °C occurred when duration of exposure was increased from 1 to 4 h. Besides, lutein loss significantly increased on rising the temperature by every 10 °C. The functional stability of lutein in relation to its degradation was also studied by monitoring its radical scavenging activity. While lutein is highly unstable, lutein structure and its respective bioactivity can be significantly (p < 0.05) retained (< 12.44% and > 54.87% respectively) by maintaining the operating conditions at higher pH (7-8) and lower temperatures (40-50 °C) for a short period of time (< 1 h). Supplementary Information: The online version contains supplementary material available at 10.1007/s13197-022-05430-3.

Physicochemical properties and angiotensin-I converting enzyme inhibitory activity of lipid-free ribbon fish (Lepturacanthus savala) protein hydrolysate.

The study aims at removal of lipid from ribbon fish protein hydrolysate (FPH) to enhance the protein content and analyse its physicochemical and bioactive properties. Ribbon fish protein hydrolysate was prepared using commercially available papain enzyme (1.5% w/v for 4 h). The resulting supernatant was further treated with lipase (0.5-2.0% w/v for 1-5 h). The treatment used in this study reduced ~ 98% of lipids depending on the enzyme concentration, temperature, pH, and duration of the treatment. Lipase treatment for 2 h increased the protein content from 62.87 to 94.11%. FPH after lipase treatment showed 1.21 folds increase in angiotensin-converting enzyme-I (ACE-I) inhibitory activity and 1.7 folds increase in standard amino acids composition (32.193 to 61.493 g/100 g). The physicochemical properties of FPH samples were analyzed by solubility, hygroscopicity, color, FT-IR, SEM, SDS-PAGE, and Zeta Potential. Use of lipase enzyme for separating the lipid content from protein hydrolysate without conferring any undesirable adverse effects on the physicochemical properties of protein hydrolysate. Lipid-free protein hydrolysates can be of commercial importance for their enhanced ACE-I inhibitory activity, replacing the side effect causing synthetic drugs for hypertension, and can have potential applications in developing functional food formulations. Supplementary Information: The online version contains supplementary material available at 10.1007/s13197-022-05620-z.

Cow ghee as an efficient carrier to improve oral bioavailability of lutein.

In India, cow-ghee has been used in traditional medicinal preparations to solubilize lipophilic drugs and enhance intestinal absorption. However, reports exploring the role of cow-ghee, naturally rich in saturated fatty acids, in carotenoid chemistry is nil. We attempted to understand the influence of fatty-acid composition of cow-ghee and edible oils on intestinal absorption of lutein in mice. The postprandial plasma lutein level in the mice administered with cow-ghee significantly (p < 0.05) reached the maximum (Cmax-135.76 pmol/mL; AUC-592.80 pmol.h/mL) within 2 h (Tmax). Cow-ghee improved oral bioavailability of lutein by 2.02, 1.41 and 1.66 folds in comparison to control, olive oil and flaxseed oil respectively. Cow-ghee, composed of 69.28% saturated fatty-acids, has the potential to be a delivery vehicle for lutein as evidenced by higher postprandial triglyceride levels. This study is first of its kind which reports the influence of saturated fatty-acids on the oral bioavailability of lutein in an in-vivo system.

Antihypertensive activity of orally consumed ACE-I inhibitory peptides.

Food proteins are sources for ACE-I inhibitory peptides that can be extracted by enzymatic hydrolysis exhibiting anti-hypertensive activity. However, these peptides are prone to further degradation by gastrointestinal enzymes during oral consumption. Bio-activity of these peptides is dependent on the resultant peptide post gastrointestinal digestion. To exhibit the bio-activity, they need to be absorbed in intact form. Although studies suggest di and tri-peptides show better ACE-I inhibitory activity, few peptides show altered IC50 values under simulated gastrointestinal digestion. Moreover, ACE-I inhibitory peptides with low IC50 values have not shown effective anti-hypertensive activity in spontaneously hypertensive rats when administered orally. Few ACE-I inhibitory peptides have reported effective reduction in systolic blood-pressure when administered through intravenously. During oral consumption of such peptides, the actual peptide sequence responsible for reducing blood-pressure is a result of breakdown in gastrointestinal tract. The fate of targeted peptides during digestion depends on amino acid sequence of the protein containing the specific site for cleavage where the action of digestive enzymes takes place. Therefore, this review attempts to explain the factors that affect the anti-hypertensive activity of ACE-I inhibitory peptides during oral consumption. It also highlights subsequent absorption of ACE-I inhibitory peptides after gastrointestinal digestion.

Genetic factors involved in modulating lutein bioavailability.

Lutein exhibits effective antioxidant activity conferring protective action against oxidative stress in age-related macular degeneration and cognitive decline. The inability to synthesize these compounds by the human body and the necessity to combat day-to-day oxidative stress prioritizes daily consumption of lutein. However, the bioavailability of the orally consumed lutein largely depends on its gastrointestinal absorption and subsequent metabolism which is in turn governed by various intrinsic and extrinsic factors. One of the most important yet least studied factors is the genetic make-up of an individual. The proteins that partake in the absorption, transportation, metabolism and excretion of lutein are encoded by the genes that experience inter-individual variability. Reports suggest that the unanimous effect of phenotypes resulting from such inter-individual variability in the genes of interest causes modulation of lutein bioavailability which is discussed in detail in this review article. However, despite the available reports, a community-based approach to a larger population is required to obtain a stronger understanding of the relationship between inter-individual variability among these genes and lutein bioavailability. Such an understanding of nutrigenetics could not only pave a way to decipher mechanisms that modulate lutein bioavailability but also help in setting the dosage requirements of each patient.

Nutraceutical approach to enhance lutein bioavailability via nanodelivery systems.

Lutein, a potent dietary carotenoid, has considerable biological activity and confers protection against age-related macular degeneration. Its bioavailability following consumption, however, depends on its rate of degradation. Nanodelivery systems with improved efficacy and stability are currently being developed to increase the bioavailability of lutein. This review examines nutraceutical approaches used in the development of such nanodelivery systems. It describes the methods of lutein preparation, the characteristics of various delivery systems, and the lutein delivery profile. In order to enhance lutein loading, provide electrostatic stabilization, and achieve the controlled release of lutein, adjuvants such as dextran moieties, whey proteins, medium-chain triglycerides, and chitosan polymers can be used to effectively reduce the particle size (< 70 nm) and improve encapsulation efficiency (to 99.5%). The improved bioavailability of lutein via nanocrystals incorporated into rapidly dissolving films for oral consumption is a new area of exploratory research. This review aims to provide clarity about current research aimed at enhancing the bioavailability of lutein through the development of nanodelivery systems.

Antihypertensive activity of fish protein hydrolysates and its peptides.

The rising interest to utilize nutritionally exorbitant fish proteins has instigated research activities in fish waste utilization. The development of newer technologies to utilize fish waste has fostered use of bioactive value-added products for specific health benefits. Enzymatically obtained Fish Protein Hydrolysate (FPH) is a rich source of biologically active peptides possessing anti-oxidant, anticancer, antimicrobial and anti-hypertensive activity. Isolating natural remedies to combat alarming negative consequences of synthetic drugs has been the new trend in current research promoting identification of antihypertensive peptides from FPH. In this review, we aim to culminate data available to produce antihypertensive peptides from FPH, its composition and potential to be used as a therapeutic agent. These purified peptides are known to be rich in arginine, valine and leucine. Reports reveal peptides with low molecular weight (<1 kDa) and shorter chain length (<20 amino acids) exhibited higher antihypertensive activity. As these peptides have proven Angiotensin Converting Enzyme - I inhibitory activity in vitro and in vivo, their potential to be used as antihypertensive drugs is outrageous. However, current focus on research in the field of molecular docking is necessary to have improved understanding of interaction of the peptides with the enzyme.

Production of bioactive hydrolysate using protease, ß-glucosidase and α-amylase of Bacillus spp. isolated from kinema.

The aim of this study was the production of soybean bioactive hydrolysate using Bacillus spp. isolated from kinema. Totally 251 bacteria isolated from kinema samples, collected at different time period were screened for protease, ß-glucosidase and α-amylase activities and further identified by ARDRA based grouping followed by analysis of 16S rRNA gene sequence similarity. The results showed that Bacillus subtilis, Bacillus amyloliquefaciens and Bacillus licheniformis were the major Bacillus species. Twelve fermentative strains belonging to these groups and having high protease, α-amylase and ß-glucosidase activity were used for solid state fermentation. The best strains for soybean fermentation that result in production of protein hydrolysates rich in polyphenols that have higher bioactivity were B. subtilis KN12C, B. amyloliquefaciens KN2G and B. licheniformis KN13C. Potential isolates can be applied for the production of soybean hydrolysates and can also find application in production of value added products from by-products of soybean processing industries.