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.

Hsp70 overexpression in Drosophila hemocytes attenuates benzene-induced immune and developmental toxicity via regulating ROS/JNK signaling pathway.

Benzene, a ubiquitous environmental chemical, is known to cause immune dysfunction and developmental defects. This study aims to investigate the relation between benzene-induced immune dysfunction and developmental toxicity in a genetically tractable animal model, Drosophila melanogaster. Further, the study explored the protective role of Heat Shock Protein 70 (Hsp70) against benzene-induced immunotoxicity and subsequent developmental impact. Drosophila larvae exposed to benzene (1.0, 10.0, and 100.0 mM) were examined for total hemocyte (immune cells) count, phagocytic activity, oxidative stress, apoptosis, and their developmental delay and reduction were analyzed. Benzene exposure for 48 h reduced the total hemocytes count and phagocytic activity, along with an increase in the Reactive Oxygen Species (ROS), and lipid peroxidation in the larval hemocytes. Subsequently, JNK-dependent activation of the apoptosis (Caspase-3 dependent) was also observed. During their development, benzene exposure to Drosophila larvae led to 3 days of delay in development, and ~40% reduced adult emergence. Hsp70-overexpression in hemocytes was found to mitigate benzene-induced oxidative stress and abrogated the JNK-mediated apoptosis in hemocytes, thus restoring total hemocyte count and improving phagocytotic activity. Further, hsp70-overexpression in hemocytes also lessened the benzene-induced developmental delay (rescue of 2.5 days) and improved adult emergence (~20%) emergence, revealing a possible control of immune cells on the organism's development and survival. Overall, this study established that hsp70-overexpression in the Drosophila hemocytes confers protection against benzene-induced immune injury via regulating the ROS/JNK signaling pathway, which helps in the organism's survival and development.

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.

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.