Addition of Pachira aquatica oil and Platonia insignis almond in cookies: Physicochemical and sensorial aspects.

This article investigated the use of Pachira aquatica (PA) fat and Platonia insignis (PI) nuts as ingredients in the preparation of cookies. Seven formulations containing PA fat and/or PI nuts were studied by changing the formulation proposed by AACC, and samples were evaluated considering physical-chemical, microbiological, and sensory characteristics. Formulations F1, F4, and F5 showed higher mass loss and lower expansion factor after cooking. Formulations F4, F6, and F7 presented a greater increase in diameter. In turn, formulations F5, F6, and F7 presented greater thickness. The content of fatty acids varied according to the composition of each biscuit, and formulations 2 and 3 presented the best lipid profile (oleic acid ~32%). In addition, it was observed that the addition of PI almond increased the fiber content (~7.15%). The sensory evaluation showed that formulation F5 obtained a score of 5, proving that the partial replacement of hydrogenated vegetable fat with PA fat and grated coconut with PI almond favored the panelists' purchasing decision. The results indicate that unconventional sources of lipids and nuts can be used without loss of quality in biscuits.

Sugarcane Juice with Co-encapsulated Bifidobacterium animalis subsp. lactis BLC1 and Proanthocyanidin-Rich Cinnamon Extract.

Bioactive compounds are sensitive to many factors, and they can alter the sensory characteristics of foods. Microencapsulation could be a tool to provide protection and allow the addition of bioactives in new matrices, such as sugarcane juice. This study focused on producing and evaluating the potential function of probiotics and proanthocyanidin-rich cinnamon extract (PRCE), both in free and encapsulated forms when added to sugarcane juice. The pure sugarcane juice treatment T1 was compared with other sugarcane juices to which bioactive compounds had been added; T2, a non-encapsulated Bifidobacterium animalis subsp. lactis (BLC1); T3, a non-encapsulated BLC1 and PRCE; T4, BLC1 microcapsules; and T5, with BLC1 and PRCE microcapsules. The samples were morphologically, physicochemically, rheologically, and sensorially characterized. Samples were also evaluated regarding the viability of BLC1 during the juice's storage at 4 °C. It was possible to produce probiotic sugarcane juice with non-encapsulated BLC1, but not with the addition of free PRCE, which in its free form reduced the viability of this microorganism to < 1 log CFU/mL after 7 days. The microcapsules were effective to protect BLC1 during juice storage and to maintain high contents of phenolic and proanthocyanidin compounds, although the products containing these had their viscosity altered and were less accepted than either the control or those with non-encapsulated BLC1.

Microencapsulation of lactase by W/O/W emulsion followed by complex coacervation: Effects of enzyme source, addition of potassium and core to shell ratio on encapsulation efficiency, stability and kinetics of release.

This study evaluated the technological viability of the formation of lactase microcapsules by coacervation (gelatin/gum arabic) containing potassium ions (cofactor). The impacts of the encapsulation and the cofactor on the enzyme properties obtained from Aspergillus oryzae and Kluyveromyces lactis were evaluated as a function of different pH values, temperatures, and storage times. The best microcapsules formed by coacervation showed good functional properties, such as low water activity (≤ 0.4) and particle size (≤ 93.52 µm), as well as high encapsulation efficiency (≥ 98.67%). The potassium ions were capable of reducing the flexibility of the polypeptide backbone, thereby increasing the stability of the enzyme. The microcapsules were also capable of increasing the stability of the enzyme under unfavorable pH values, high temperatures and during storage. An in vitro experiment showed that microcapsules were effective in the retention of about 90% of the enzyme in simulated gastric fluid, but as much as 95% of the enzyme can be released from the capsules in simulated intestinal fluid. The released enzyme retained 83% and 66% of the total enzymatic activity for the capsules produced with lactase from Kluyveromyces lactis and A. oryzae, respectively. These results are promising and demonstrated that these microcapsules are a promising technology to protect and deliver bioactive proteins during storage and delivery in the GI tract.

Immobilization of ß-galactosidase by complexation: Effect of interaction on the properties of the enzyme.

In the present work, we aimed to explore the molecular binding between alginate and ß-galactosidase, as well as the effect of this interaction on the activity retention, thermal stability, and kinetic properties of the enzyme. The impact of pH and enzyme/alginate ratio on physicochemical properties (turbidity, morphology, particle size distribution, ζ-potential, FTIR, and isothermal titration calorimetry) was also evaluated. The ratio of biopolymers and pH of the system directly affected the critical pH of complex formation; however, a low alginate concentration (0.1 wt%) could achieve an electrical charge equivalence at pH 3.4 with 93.72% of yield. The binding between ß-galactosidase and alginate was an equilibrium between enthalpic and entropic contributions, which promoted changes in the structure of the enzyme. Nevertheless, this conformational modification was reversible after the dissociation of the complex, which allowed the enzyme to regain its activity. These findings will likely broaden functional applications of enzyme immobilization.

Interpolymer complexation of egg white proteins and carrageenan: Phase behavior, thermodynamics and rheological properties.

The complexation between lysozyme/carrageenan and ovalbumin/carrageenan was studied in situ using acidification. The complexes were analyzed in solutions with different NaCl concentrations and different protein/polysaccharide ratios. As the protein/polysaccharide ratio increased from 1:1 to 10:1, critical structure forming events (i.e., those associated with soluble, insoluble and large insoluble complexes) shifted to higher pH values for ovalbumin/carrageenan followed by decrease of G' values at ratios of 5:1 and 10:1. The increase in the ratio of lysozyme/carrageenan complexes suppressed the critical pH transition points that led to the formation of large insoluble complexes from pH 12.0 until 1.0, and the values of G' increased simultaneously, reaching the highest value at a ratio of 10:1. Addition of salt to the ovalbumin/carrageenan and lysozyme/carrageenan mixtures suppressed the electrostatic interaction between proteins and carrageenan at lower pH values and the critical pH transitions points, whereas at a ratio of 3:1 with a 0.01 M concentration, the coacervate yield of the complex reached 79.6% ±â€¯0.6 and 93.7% ±â€¯4.8 for the ovalbumin and lysozyme complexes, respectively. The rheological data associated with microscopy images show that interpolymer complexes with heterogeneous structures were formed for both complexes, and we suggest that complexes have a great potential to improve or extend the texture, mechanical stability, consistency, and taste of food products.

Complex coacervation between lysozyme and pectin: Effect of pH, salt, and biopolymer ratio.

The complexation between lysozyme and pectin was studied by acidification using zeta potential, turbidity measurements and calorimetry titration. The complexes were analyzed in various NaCl concentrations with different ratios. At ratio 1:1 with 0.01M NaCl, is worth mentioning that the insoluble complexes were formed between pH 2.0 and 7.0, which represents a great range to apply this complex to different food matrices. When the ratio was increased from 1:1 to 3:1, the pH range between the pHφ1 and pHφ2 increased even more. When the NaCl concentration was increased from 0.01M to 0.2M, a progressive reduction of turbidity was observed. At 0.4M NaCl, there was total suppression of complex formation at ratio ≤ 3:1. The process of complex coacervate formation occurred in two different steps, presenting favorable enthalpic as well as entropic contributions. The positive entropy change is a strong indication that water molecules have been released from the complex surface, however the positive sign of TΔS suggests that hydrophobic interactions were involved in the interaction between lysozyme and pectin. Microscopy images of the samples revealed that the complexes presented a spheroid-like appearance which may contribute to possible future applications.

Complex coacervates obtained from peptide leucine and gum arabic: formation and characterization.

In this study, interactions between polypeptide-leucine (0.2% w/w) and gum arabic (0.03, 0.06, 0.09, 0.12, and 0.15% w/w) were examined at concentrations of NaCl (0, 0.01, 0.25, 0.3, 0.5mol/l) and at different pH values (from 1.0 to 12.0). Formation of insoluble complex coacervates was highest at pH 4.0. At pH 2.0, which is the pKa of the gum Arabic, the dissociation of precipitate occurred. The pHØ2 positively shifted with the addition of higher concentrations of salt. Samples containing 0.2% PL and 0.03% GA and no salt had higher turbidity and increased formation of precipitates showing greater turbidity and particle sizes. The Fourier transform infrared spectroscopy confirms the complex coacervate formation of leucine and gum arabic, and rheological measurements suggest the elastic behavior of 0.2% PL and 0.03% GA complex. Overall, the study suggests that complex coacervates of PLs could be one feasible ways of incorporating amino acids in food products.