Banana peel nanocellulose and soy protein hydrolysate complexed colloidal nanoparticles synthesis using ultrasonic interventions: characterization and stable pickering emulsion formation.

Pickering based emulsion system are been gaining interest in active delivery of encapsulated molecules in food system. In the present study, cellulose nanoparticles (CNPs) were isolated from food waste (banana peel) using acid hydrolysis followed by high-intensity ultrasonication. The complex colloidal nanoparticles (CNPSPH) were fabricated using hydrogen bonding and electrostatic interactions between cellulose nanoparticles and soy protein hydrolysates. With 400 W power level for 30 min, size of 53.11 ± 1.45 nm with polydispersity index of 0.21 ± 0.21 and Zeta potential of - 34.33 ± 0.77 were noted for generated CNPs. The three-phase contact angle (o/w) of CNPSPH at a mass ratio of 1:1 CNPs to SPHs (CNPSPH 1:1) was approximately 89.07°, indicating as effective Pickering emulsifiers. Furthermore, the stability of the Pickering emulsion stabilised by CNPSPH complex was investigated under various pH and temperature conditions. The findings will provide solution in development of nanocellulose-soy protein complex particles for a stabilized Pickering emulsion formation. Supplementary Information: The online version contains supplementary material available at 10.1007/s10068-023-01477-w.

Sonochemical effect on the degree of substitution of octenyl-succinic anhydride into waxy rice starch nanoparticles and study of gastro-intestinal hydrolysis using INFOGEST in vitro digestion method.

Octenyl succinylation of starch nanoparticles has been proven to be effective in a variety of food industry applications such as fat replacement, thickening agents, emulsion formation, and delivery of bioactive compounds. In this study, waxy rice starch was debranched with pullulanase to obtain short glucans, which were then modified with octenyl succinic anhydride (OSA) to obtain amphiphilic short glucans (ASG) using high (400 W) and low (200 W) ultrasonic power intensity at 30 and 60 cycles. Developed ASG were characterized by nanoparticle size (ca. < 50 nm), surface hydrophobicity and gastro-intestinal stability. Ultrasonic intervention progressively increased the degree of substitution (DS) of OSA into hydrolysed starch. A significant molecular exchange between starch and OSA was confirmed with shoulder peak at 1.07 ppm by 1H NMR, and 1560 and 1727 cm-1 peaks in FTIR spectral image, and broad band at 1260 cm-1 by Raman spectroscopy. The XRD analysis confirmed the change in crystalline structure, and the emergence of new peaks at 2θ angles of around 5.81° which represent the development of B-type structure following pullulanasehydrolysis, and minor peaks at 13.92° and 19.83°, which imply the production of Vh type structures in ASG. Gastro-intestinal hydrolysis of starch after modification was analyzed in a sequential digestion process using INFOGEST method. The gastro-kinetic studies unveiled the reduction in the digestibility constant in the oral-gastric phase, with significantly enhanced value of kinetic constants in the intestinal phase, proving a sustained gastro-intestinal stability. The OSA-modified starches with greater DS havemore rigid and compact surface structure, which provides superior protection against biochemical conditions in the stomach fluid.

Inhibition mechanism of 3-hydroxy-3-methyl-glutaryl-CoA reductase by tocotrienol-rich rice bran fraction optimally extracted with ultrasonic energy.

Tocotrienols (T3) are vitamin E components that inhibit 3-hydroxy-3-methyl-glutaryl-CoA reductase (HMGR), a primary target for cholesterol management. T3 was extracted from rice bran (RBE) using ultrasonic energy keeping solute: solvent ratio, power and time on specific energy and T3 concentration as responses as per Box-Behnken Design. The lowest specific energy (52.38 ± 0.14 J mL-1) uptake by the sample was most effective in enhancing the concentration of T3 in RBE (199.34 ± 0.63 µg mL-1). In vitro HMGR kinetics and in silico binding interactions of the identified α-, δ- and γ-T3 fractions were studied. Enzyme kinetic studies revealed an uncompetitive mode of inhibition by α-T3, γ-T3, and RBE and a mixed mode of inhibition for δ-T3. γ-T3 showed lowest IC50 concentration (11.33 µg mL-1) followed by α-T3 (16.73 µg mL-1), RBE (20.45 µg mL-1) and δ-T3 (23.16 µg mL-1). Molecular docking studies highlighted the hydrogen bonding of δ-T3 with Gln766 and α- and γ-T3 with Met655 and Val805 amino acid residues at the NADPH binding site of HMGR. Results indicate the potential use of T3 enriched RBE optimally extracted using ultrasound as potent HMGR inhibitor.