RESULT: Pea and rice bran proteins both enhanced emulsion stability. Pea protein enhanced the viscosity of the continuous phase whereas rice bran protein lowered interfacial tension. When applied synergistically, competitive adhesion occurred. Rice bran protein gradually displaced pea protein from the oil droplet surface as its concentration increased, leading to emulsion destabilization due to the displaced pea protein. The use of high-pressure homogenization further enhanced the stability of the emulsion by unfolding protein partially. However, increasing homogenization pressure (>500 Bar) and homogenization cycle (>2 cycles) led to protein aggregation due to excessive exposure of its hydrophobic core. The emulsion formed was resistant to coalescence at 4 °C for 28 days and was stable under high pH and low ionic conditions.
CONCLUSION: The synergistic combination of plant proteins and the effective utilization of co-processing (homogenization) can enhance the functionality of the individual proteins significantly, leading to the formation of a stable emulsion. The use of plant protein mixture as a stabilizer not only improved the emulsion stability but also ensured a plant-based beverage with a complete amino acid profile for the vegan community. © 2024 The Author(s). Journal of the Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.
RESULTS: All EPH samples revealed induction effects towards Bifidobacterium spp., Lactobacillus-Enterococcus and Bacteroidaceae/Prevotellaceae populations similar to those in inulin fermentation. A significant decrease (P ≤ 0.05) in pathogenic Clostridium histolyticum group was observed in the response of raw sago palm hearts. In general, all samples stimulate the production of SCFA. Particularly in the colonic fermentation of sago palm heart, acetate and propionate revealed the highest concentrations of 286.18 and 284.83 mmol L-1 in raw and cooked form, respectively.
CONCLUSION: This study concluded that edible palm hearts can be a potential prebiotic ingredient that promotes human gastrointestinal health, as well as discovering a new direction towards an alternative source of functional foods. © 2022 Society of Chemical Industry.
RESULTS: A maximum protein yield of 12.05 g/100 g with purity level 91.94 g/100 g was obtained using an optimized extraction with pH 11.0, seed:water ratio 50:1, 360 min duration, and temperature 50 °C. The oil and water retention capacities of KSPI were 1.14 mL g-1 and 1.37 mL g-1 respectively. After 30 min at pH 7, KSPIs demonstrated remarkable emulsion capacity (83.12%) and stability (75.63%), along with high foaming capacity (106%) and stability (18.3%). As per high-performance liquid chromatography analysis, arginine, glutamic acid, leucine, phenylalanine, and lysine were the most abundant amino acids detected in KPSIs. The KSPIs' globular protein structure was successfully verified using analytical approaches, including Fourier transform infrared spectroscopy, protein fraction ratios, and differential scanning calorimetry. Sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis revealed that KPSI has a molecular weight distribution ranging from 10 kDa to 50 kDa.
CONCLUSION: The results of this study support the application of the proposed response-surface-methodology-optimized extraction method for efficient recovery of high-quality kenaf seed proteins that meet the necessary physicochemical and techno-functional requirements. © 2024 Society of Chemical Industry.