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1.
Foods ; 13(13)2024 Jul 01.
Article in English | MEDLINE | ID: mdl-38998597

ABSTRACT

Plant-based protein is considered a sustainable protein source and has increased in demand recently. However, products containing plant-based proteins require further modification to achieve the desired functionalities akin to those present in animal protein products. This study aimed to investigate the effects of enzymes as cross-linking reagents on the physicochemical and functional properties of hybrid plant- and animal-based proteins in which lupin and whey proteins were chosen as representatives, respectively. They were hybridised through enzymatic cross-linking using two laccases (laccase R, derived from Rhus vernicifera and laccase T, derived from Trametes versicolor) and transglutaminase (TG). The cross-linking experiments were conducted by mixing aqueous solutions of lupin flour and whey protein concentrate powder in a ratio of 1:1 of protein content under the conditions of pH 7, 40 °C for 20 h and in the presence of laccase T, laccase R, or TG. The cross-linked mixtures were freeze-dried, and the powders obtained were assessed for their cross-linking pattern, colour, charge distribution (ζ-potential), particle size, thermal stability, morphology, solubility, foaming and emulsifying properties, and total amino acid content. The findings showed that cross-linking with laccase R significantly improved the protein solubility, emulsion stability and foaming ability of the mixture, whereas these functionalities were lower in the TG-treated mixture due to extensive cross-linking. Furthermore, the mixture treated with laccase T turned brownish in colour and showed a decrease in total amino acid content which could be due to the enzyme's oxidative cross-linking mechanism. Also, the occurrence of cross-linking in the lupin and whey mixture was indicated by changes in other investigated parameters such as particle size, ζ-potential, etc., as compared to the control samples. The obtained results suggested that enzymatic cross-linking, depending on the type of enzyme used, could impact the physicochemical and functional properties of hybrid plant- and animal-based proteins, potentially influencing their applications in food.

2.
J Dairy Sci ; 2024 Jun 20.
Article in English | MEDLINE | ID: mdl-38908705

ABSTRACT

The production of whey protein concentrates (WPCs) from camel milk whey represents an effective approach to valorize this processing by-product. These concentrates harbor active ingredients with significant bioactive properties. Camel WPCs were spray-dried (SD) at inlet temperature of 170, 185 and 200°C, or Ultrasonicated (US) for 5, 10 and 15 min, then freeze-dried to obtain fine powder. The impact of both treatments on protein degradation was studied by sodium dodecyl sulfate-PAGE and reverse-phase ultraperformance liquid chromatography (RP-UPLC) techniques. Significantly enhanced protein degradation was observed after US treatment when compared with SD. Both SD and US treatments slightly enhanced the WPCs samples' antioxidant activities. The US exposure for 15 min exhibited highest 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) scavenging activity (12.12 mmol TE/g). Moreover, US treatment for 10 min exhibited the highest in vitro anti-diabetic properties (α-amylase and α-glucosidase inhibition), and dipeptidyl-peptidase-IV inhibitory activity among all samples. In addition, the ultrasonication for 10 min and SD at 170°C showed the lowest IC50 values for in vitro anti-hypercholesterolemic activities in terms of pancreatic lipase and cholesteryl esterase inhibition. Conclusively, these green techniques can be adapted in the preservation and processing of camel milk whey into active ingredients with high bioactive properties.

3.
Biomed Mater ; 19(4)2024 Jun 28.
Article in English | MEDLINE | ID: mdl-38857605

ABSTRACT

Chronic skin wounds pose a global clinical challenge, necessitating effective treatment strategies. This study explores the potential of 3D printed Poly Lactic Acid (PLA) scaffolds, enhanced with Whey Protein Concentrate (WPC) at varying concentrations (25, 35, and 50% wt), for wound healing applications. PLA's biocompatibility, biodegradability, and thermal stability make it an ideal material for medical applications. The addition of WPC aims to mimic the skin's extracellular matrix and enhance the bioactivity of the PLA scaffolds. Fourier Transform Infrared Spectroscopy results confirmed the successful loading of WPC into the 3D printed PLA-based scaffolds. Scanning Electron Microscopy (SEM) images revealed no significant differences in pore size between PLA/WPC scaffolds and pure PLA scaffolds. Mechanical strength tests showed similar tensile strength between pure PLA and PLA with 50% WPC scaffolds. However, scaffolds with lower WPC concentrations displayed reduced tensile strength. Notably, all PLA/WPC scaffolds exhibited increased strain at break compared to pure PLA. Swelling capacity was highest in PLA with 25% WPC, approximately 130% higher than pure PLA. Scaffolds with higher WPC concentrations also showed increased swelling and degradation rates. Drug release was found to be prolonged with increasing WPC concentration. After seven days of incubation, cell viability significantly increased in PLA with 50% WPC scaffolds compared to pure PLA scaffolds. This innovative approach could pave the way for personalized wound care strategies, offering tailored treatments and targeted drug delivery. However, further studies are needed to optimize the properties of these scaffolds and validate their effectiveness in clinical settings.


Subject(s)
Bandages , Biocompatible Materials , Polyesters , Printing, Three-Dimensional , Tensile Strength , Tissue Scaffolds , Whey Proteins , Wound Healing , Whey Proteins/chemistry , Polyesters/chemistry , Tissue Scaffolds/chemistry , Wound Healing/drug effects , Humans , Biocompatible Materials/chemistry , Materials Testing , Spectroscopy, Fourier Transform Infrared , Microscopy, Electron, Scanning , Cell Survival/drug effects , Porosity , Drug Liberation , Skin/metabolism
4.
Food Sci Nutr ; 12(5): 3273-3281, 2024 May.
Article in English | MEDLINE | ID: mdl-38726417

ABSTRACT

Oleogel is a viscoelastic, spreadable and semi-solid structure, which is used as a fat substitute and a controller the release of bioactive compounds. The aim of this study was to develop low fat dairy dessert enriched with berberine with applying oleogel system as delivery system and fat replacer. The oleogel prepared with an emulsion-templated methods based on soluble interaction of whey protein concentrate (WPC), WPC-basil seed gum (BSG), and WPC-xanthan gum (XG). In the first step, berberine release kinetic in in-vitro gastrointestinal environment was studied. The results showed that the mouth environment had the highest release rate of berberine. Cooperation of hydrocolloids in oleogel increase stability of structure in stomach condition in compared with WPC oleogel. The suitable model to fit the oleogels contain beberine was the Korsmeyer-Papas that was the highest R 2 (.98). According to release results of berberine from oleogel network, the oleogel 0.6BSG:WPC was chosen and applied in formulation of dairy dessert at different levels (0%, 25%, 50%, 75% and 100% of oleogel) instead of cream. The dessert contained uncoated berberine had the unacceptable bitterness in comparison with samples containing coated berberine with oleogel. The overall acceptance decreased with increment of oleogel due to increasing of bitter taste. Appling berberine (therapeutic compound) and oleogel (fat-substitute) to achieve marketable consumer products showed positive effects on trend of the study, especially at low level of substitution.

5.
Int J Biol Macromol ; 271(Pt 1): 132512, 2024 Jun.
Article in English | MEDLINE | ID: mdl-38795879

ABSTRACT

Emulsion micro-gels exhibit significant potential as functional ingredients for modifying food texture, replacing saturated fats, or serving as templates for the controlled release of bioactive compounds. Structural design principles are being applied more frequently to develop innovative emulsion micro-gels. In this paper, whey protein concentrate (WPC), κ-carrageenan and sodium alginate (SA) were utilized for preparing emulsion micro-gels. To reveal the regulation mechanism of the structural and physicochemical properties of emulsion micro-gels on lipid digestion, the influence of SA additions on the structural, physicochemical properties and in vitro digestion behavior of κ-carrageenan/WPC-based emulsion micro-gel were explored. The FTIR results suggest that the emulsion micro-gels are formed through non-covalent interactions. With the increase of SA addition (from 0.7 g/100 mL to 1.0 g/100 mL), the decreased mean droplet size, the increased hardness, elasticity indexes, and water holding capacity, the reduced the related peak times all indicated that the emulsion micro-gels exhibit enhanced rheological, stability, and mechanical properties. It can be concluded from the microstructure, particle size distribution of the emulsion micro-gels during simulated digestion and free fatty acid release that both κ-carrageenan/WPC-based emulsion micro-gel and κ-carrageenan/WPC/SA-based emulsion micro-gel can inhibit lipid digestion due to the ability to maintain structural stability and hindering the penetration of bile salts and lipase through the hydrogel networks. And the ability is regulated by the binding properties the gel matrix and oil droplets, which determine the structure and physicochemical properties of emulsion micro-gels. The research suggested that the structure of emulsion micro-gels can be modified to produce various lipid digestion profiles. It may be significant for certain practical application in the design of low-fat food and controlled release of bioactive agents.


Subject(s)
Alginates , Carrageenan , Emulsions , Whey Proteins , Whey Proteins/chemistry , Carrageenan/chemistry , Alginates/chemistry , Emulsions/chemistry , Rheology , Gels/chemistry , Digestion/drug effects , Chemical Phenomena , Particle Size
6.
Food Chem ; 449: 139310, 2024 Aug 15.
Article in English | MEDLINE | ID: mdl-38608612

ABSTRACT

This study investigated the effects of the conjugate reaction sequences of whey protein concentrate (WPC), epigallocatechin gallate (EGCG) and dextran (DEX) on the structure and emulsion properties of conjugates and the bioaccessibility of astaxanthin (AST). Two types of ternary covalent complexes were synthesised using WPC, EGCG and DEX, which were regarded as emulsifiers of AST nanoemulsions. Results indicated that the WPC-DEX-EGCG conjugate (referred to as 'con') exhibits a darker SDS-PAGE dispersion band and higher contents of α-helix (6%), ß-angle (24%) and random coil (32%), resulting in a greater degree of unfolding structure and fluorescence quenching. These findings suggested WPC-DEX-EGCG con had the potential to exhibit better emulsification properties than WPC-EGCG-DEX con. AST encapsulation efficiency (76.22%) and bioavailability (31.89%) also demonstrated the superior performance of the WPC-DEX-EGCG con emulsifier in nanoemulsion delivery systems. These findings indicate that altering reaction sequences changes protein conformation, enhancing the emulsification properties and bioavailability of AST.


Subject(s)
Biological Availability , Catechin/analogs & derivatives , Emulsifying Agents , Emulsions , Whey Proteins , Xanthophylls , Xanthophylls/chemistry , Emulsions/chemistry , Emulsifying Agents/chemistry , Whey Proteins/chemistry , Animals , Catechin/chemistry , Dextrans/chemistry , Male , Rats , Rats, Sprague-Dawley
7.
Foods ; 13(6)2024 Mar 07.
Article in English | MEDLINE | ID: mdl-38540812

ABSTRACT

The selection of appropriate probiotic strains is vital for their successful inclusion in foods. These strains must withstand processing to reach consumers with ≥106 CFU/g, ensuring effective probiotic function. Achieving this in commercial products is challenging due to sensitivity to temperature during processing. In this work, Lactobacillus reuteri DSM 17938 was microencapsulated by ionic gelation (with alginate or pectin) followed by polymeric coating (with whey protein concentrate or chitosan). Then, such microcapsules were incorporated into a strawberry puree, which was subsequently dehydrated at three temperatures (40 °C, 45 °C, and 50 °C) by Refractance Window®. The ultimate aim was to demonstrate the efficacy of the proposed methods from a technological point of view. Kinetic curves of the probiotic's viability showed a high cell loading (>109 CFU/g). Additionally, an average encapsulation efficiency of 91% and a particle size of roughly 200 µm were found. A decrease in the viability of the microorganism was observed as drying temperature and time increased. As a demonstration of the above, in a particular case, drying at 45 °C and 50 °C, viable cells were found up to 165 min and 90 min, respectively; meanwhile, drying at 40 °C, viable cells were reported even after 240 min. The greatest viability preservation was achieved with Refractance Window® drying at 40 °C for 240 min when microcapsules coated with whey protein concentrate were incorporated into puree; this procedure showed great potential to produce dehydrated strawberry snacks with moisture (15%), water activity (aw < 0.6), and viability (≥106 CFU/g) suitable for functional foods. The membrane-stabilizing properties of whey protein concentrate could prevent cell damage. In contrast, probiotics in chitosan-coated capsules showed reduced viability, potentially due to antimicrobial properties and the formation of cracks. These findings signify a breakthrough in the production of dehydrated snacks with the addition of probiotics, addressing challenges in preserving the viability of these probiotics during processing; thus, opening the possibility for the development of a probiotic strawberry snack.

8.
Food Sci Nutr ; 12(3): 1655-1672, 2024 Mar.
Article in English | MEDLINE | ID: mdl-38455175

ABSTRACT

The impacts of pH (2.8, 4.5, and 7.2) and extrusion cooking temperature (60°C, 85°C, and 110°C) on properties of native whey protein concentrate (NWPC) were evaluated, followed by delivering of curcumin through a nanoemulsion system stabilized with extruded WPC (EWPC). Protein solubility, surface hydrophobicity, and emulsion properties such as emulsion activity index (at 1% [w/w] protein concentration), stability index (at 0.5%, 1%, 2%, and 4% [w/w] protein concentration) and creaming index (evaluated at different protein concentrations [0.5%, 1%, 2%, and 4% w/w] and oil levels [20%, 40%, 60%, and 80%]) were improved as a function of the extrusion process. It was found that both covalent and non-covalent interactions contributed to the stabilization of the extrudates. The rheological investigation of the emulsions stabilized with EWPC (at different oil levels [20%, 40%, 60%, and 80%]) revealed high viscosity and shear thinning behavior as well as much higher G' and G″ values. Encapsulation efficiency was increased from 90.8% to 95.7% when NWPC and EWPC were used, respectively. The curcumin-loaded nanoemulsion containing EWPC presented high stability in confronting with ionic strength (NaCl salt with a concentration of 0.1-1 M), pH (3, 5, and 7), thermal treatments (pasteurization at 63°C for 30 min and sterilization at 95°C for 10 min) and storage time (1 month at 4°C and 25°C). In vitro release behavior revealed that samples stabilized with EWPC showed burst release in simulated intestine conditions. However, it was more stable in stomach conditions.

9.
Food Sci Nutr ; 11(11): 6907-6919, 2023 Nov.
Article in English | MEDLINE | ID: mdl-37970390

ABSTRACT

Applying hydrocolloids in the structure of protein emulsion gel can improve its properties. Interaction of whey protein concentrate (WPC) (5%) with xanthan gum (XG) and basil seed gum (BSG) at different concentrations (0.2%, 0.4%, and 0.6%) was investigated to improve mechanical and structural properties of emulsion gel. Results illustrated that gums created a stronger structure around the oil droplets, which confocal images approved it. Also, the particle size decreased and uniformed by cooperating 0.6% gum in comparison with WPC (46.87 µm). The lowest and highest hardness values were observed in emulsion gel formed by WPC (1.27 N) and 0.6BSG: WPC (3.03 N), respectively. Also, the increase of gum concentration had a positive on consistency parameter of texture, so the value was 11.48 N s in WPC emulsion gel and it reached 0.6BSG: WPC (25.71 N s) and 0.6XG: WPC (19.96 N s). Evaluating the stability of the treatments by centrifugation indicated that 0.6BSG: WPC (89.10%) and 0.6XG: WPC (74%) had the highest level of stability. Increasing gum concentration increased the consistency and viscosity. Also, the viscoelastic properties of emulsion gel improved by 0.6% BSG. The elastic modulus of the WPC, 0.6XG: WPC, and 0.6BSG: WPC emulsion gels at the same frequency (1 Hz) was 240.90, 894.59, and 1185.61 Pa, respectively. In general, the interaction of WPC solution with hydrocolloids, especially BSG, is suggested to prepare more stable and elastic emulsion gels.

10.
Food Res Int ; 174(Pt 1): 113572, 2023 12.
Article in English | MEDLINE | ID: mdl-37986444

ABSTRACT

Yeast protein concentrate, a by-product of the fermentation industry waste, is a potential alternative protein source with high nutritional quality, environmental sustainability, and functional properties. However, its digestibility and digestion behavior are poorly understood. In this study, we compared the in vitro digestion behavior of yeast protein concentrate and whey protein concentrate using simulated gastrointestinal conditions. We found that yeast protein concentrate had lower digestibility than whey protein concentrate (31.25% vs. 86.23% at 120 min of pepsin digestion and 75.12% vs. 95.2% at 120 min of pancreatin digestion). Yeast protein concentrate differed from whey protein concentrate in microstructure, secondary structure, and amino acid composition, which may affect its digestion behavior. Compared to whey protein concentrate, a higher level of ß-sheets and a lower zeta potential explain the slow-digesting property of yeast protein concentrate. Yeast protein concentrate also underwent depolymerization and Plastein reaction during digestion. These results provided valuable information for developing and applying yeast protein concentrate as an alternative to conventional animal protein.


Subject(s)
Digestion , Saccharomyces cerevisiae , Animals , Whey Proteins/metabolism , Saccharomyces cerevisiae/metabolism , Amino Acids/metabolism , Fungal Proteins
11.
J Food Sci Technol ; 60(12): 2916-2926, 2023 Dec.
Article in English | MEDLINE | ID: mdl-37786599

ABSTRACT

Starches and proteins are two major types of biopolymer components in many foods. The interactions of protein with starches greatly influence the matrix structure and properties of starch-based food systems. In this study, the physical-chemical properties and the effect of the commercial whey protein concentrate in the texture and rheological properties of jackfruit starch gels were evaluated. The experimental design was completely randomized, using a 4 × 4 complete factorial scheme, with four levels of starch (3, 6, 9 and 12%) and four levels of protein (0, 2, 4 and 6%). In higher concentrations of starch the addition of proteins delayed the beginning of gelatinization, led to an increase in G' and G″ and decrease in the tan (δ) values, characterizing the gel as strong, e.g., the gel network became more structured. However, in the treatment with 6% starch the addition of protein led to a decrease in gel strength. For gels with 9% starch the increase in protein concentration, led a slight increase in the hardness and cohesiveness, characterizing a more rigid and cohesive gel. Overall, gels with 3 and 6% of starch showed characteristic behavior of a weak gel and with 9 and 12% of strong gel. Supplementary Information: The online version contains supplementary material available at 10.1007/s13197-023-05793-1.

12.
Foods ; 12(20)2023 Oct 17.
Article in English | MEDLINE | ID: mdl-37893698

ABSTRACT

The main aim of the study was to establish the impact of limited proteolysis by actinidin on the functionality of selected milk protein systems. The plant protease actinidin was used to produce hydrolysates (MPHs) from milk protein concentrate (MPC) and whey protein concentrate (WPC) to 0, 5, 10 or 15% of the degree of hydrolysis (DH) at an enzyme-to-substrate ratio of 1:100 (5.21 units of actinidin activity g-1 of protein). The functionalities assessed included solubility, heat stability, emulsification and foaming properties. In general, significant changes in the functionalities of MPH were associated with the extent of hydrolysis. Solubility of hydrolysates increased with increasing %DH, with WPC showing about 97% solubility at 15% DH. Emulsifying properties were negatively affected by hydrolysis, whereas heat stability was improved in the case of WPC (~25% of heat stability increased with an increase in DH to 15%). Hydrolysates from both WPC and MPC had improved foaming properties in comparison to unhydrolysed controls. These results were also supported by changes in the FTIR spectra. Further adjustment of hydrolysis parameters, processing conditions and pH control could be a promising approach to manipulate selected functionalities of MPHs obtained using actinidin.

13.
Polymers (Basel) ; 15(15)2023 Aug 06.
Article in English | MEDLINE | ID: mdl-37571210

ABSTRACT

Anthocyanins (ANs) have strong antioxidant activities and can inhibit chronic diseases, but the instability of ANs limits their applications. The conservation of preheating whey protein concentrate (WPC) on the stability of purple sweet potato ANs was investigated. The retention of ANs in WPC-ANs was 85.88% after storage at 25 °C for 5 h. WPC-ANs had higher retention of ANs in heating treatment. The retention rates of ANs in WPC-ANs exposed to light and UV lamps for 6 h were 78.72% and 85.76%, respectively. When the concentration of H2O2 was 0.50%, the retention rate of ANs in the complexes was 62.04%. WPC-ANs' stability and antioxidant activity were improved in simulated digestive juice. The WPC-ANs connection was static quenching, and the binding force between them was a hydrophobic interaction at one binding site, according to the fluorescence quenching spectroscopy. UV-visible absorption spectroscopy and Fourier transform infrared spectroscopy (FTIR) analysis further indicated that the secondary structure and microenvironment of amino acid residues in WPC can be impacted by the preheating temperature and preheating times of WPC. In conclusion, preheating WPC can successfully preserve the stability of purple sweet potato ANs by binding to them through a non-covalent interaction.

14.
J Food Sci Technol ; 60(9): 2408-2422, 2023 Sep.
Article in English | MEDLINE | ID: mdl-37424588

ABSTRACT

The study's objectives were to develop a packaging film incorporating oregano essential oil, and evaluate the antioxidant, antibacterial, mechanical, and physicochemical activities of the film toward grapes packaging. The films were developed by casting method, after adding nano-emulsion of essential oil into WPC-glycerol film forming solution. The effects of the Oregano Essential Oil (OEO) at different concentrations of 1, 2, 3, and 4% (w/w) in the WPC edible films were studied. The light transmittance, colour aspects, water aspects, mechanical, antioxidant, antimicrobial activities, FTIR, SEM microstructure, and biodegradability of the film were studied. Acidity, weight, TSS, pH and 9-point hedonic sensory analysis of grapes packed in WPC-OEO film were evaluated. Results showed that 3% OEO incorporated WPC film displayed positive inhibition towards pathogenic bacteria; Staphylococcus aureus and Escherichia coli (25.36 ± 0.52-28.0 ± 0.5 mm), the antioxidant activity of 86.89 ± 0.087% and 51.24 ± 0.031% for DPPH, FRAP respectively and degradation after 10 days. The film displayed reduced light transmittance, lower water solubility (44.04 ± 2.361%) and prominent surface characteristics in SEM microstructure and FTIR spectra. The grapes packed in WPC-3% OEO film were firmer, had less surface colour change and showed negligible change in weight, pH, acidity, and Brix value throughout the storage period. Thus, the developed film displayed excellent antibacterial and antioxidant properties that potentially extended the quality of fresh grapes during refrigerated storage. Supplementary Information: The online version contains supplementary material available at 10.1007/s13197-023-05763-7.

15.
Microorganisms ; 11(7)2023 Jul 03.
Article in English | MEDLINE | ID: mdl-37512914

ABSTRACT

Three Streptococcus thermophilus strains, namely RBC6, RBC20, and RBN16, were proven to release bioactive peptides during whey protein concentrate (WPC) fermentation, resulting in WPC hydrolysates with biological activities. However, these bioactive peptides can break down during gastro-intestinal digestion (GID), hindering the health-promoting effect of fermented WPC hydrolysates in vivo. In this work, the effect of simulated GID on three WPC hydrolysates fermented with S. thermophilus strains, as well as on unfermented WPC was studied in terms of protein hydrolysis, biological activities, and peptidomics profiles, respectively. In general, WPC fermentation enhanced protein hydrolysis compared to unfermented WPC. After in vitro GID, WPC fermented with S. thermophilus RBC20 showed the highest antioxidant activity, whereas WPC fermented with strain RBC06 displayed the highest angiotensin-converting enzyme (ACE)- and dipeptidyl peptidase IV (DPP-IV)-inhibitory activities. Peptidomics analysis revealed that all digested WPC samples were highly similar to each other in peptide profiles, and 85% of the 46 identified bioactive peptides were shared among fermented and unfermented samples. However, semi-quantitative analysis linked the observed differences in biological activities among the samples to differences in the amount of bioactive peptides. The anti-hypertensive peptides VPP and IPP, as well as the DPP-IV-inhibitory peptide APFPE, were quantified. In conclusion, WPC fermentation with S. thermophilus positively impacted protein hydrolysis and bioactive peptide release during GID.

16.
J Food Sci ; 88(7): 2996-3006, 2023 Jul.
Article in English | MEDLINE | ID: mdl-37306525

ABSTRACT

The effect of l-arginine (Arg) on the thermal stability of whey protein-corn oil emulsions was investigated to determine its role in improving emulsion stability. The results indicated that with an increase in Arg concentration, the emulsion stability index, emulsification activity index, and absolute ζ-potential increased initially and decreased after high-temperature sterilization. However, the mean particle size, apparent viscosity, creaming indices, and dynamic interfacial pressure of the emulsions first decreased and then increased, and the performance of samples that only showed an increase in pH could also improve the emulsification stability. These results clarify the mechanism by which Arg increases the thermal stability of emulsions.


Subject(s)
Corn Oil , Water , Emulsions , Whey Proteins , Particle Size , Rheology
17.
Foods ; 12(11)2023 May 26.
Article in English | MEDLINE | ID: mdl-37297408

ABSTRACT

The production of cream cheese, curd, high-protein yogurt, or caseinate results in large amounts of acid whey as a by-product. So far acid whey is often disposed as animal feed or organic fertilizer. However, these approaches ignore the valorization potential that arises from the unique composition of the whey protein fraction. Whey contains the biofunctional proteins lactoferrin and immunoglobulin G, which possess immune-supporting, antibacterial, antiviral, and numerous further health-promoting functions. However, the concentration of these proteins in bovine milk or whey is below a physiologically relevant level. Based on literature research we specified a daily intake of 200 mg lactoferrin as the minimal functional dose. By means of cross-flow ultrafiltration, an attempt was made to increase the concentration of biofunctional proteins. Therefore, a membrane for the selective retention of lactoferrin and immunoglobulin G was identified, and the process parameters were optimized. Finally, a concentration experiment was conducted, whereby the concentration of biofunctional proteins was increased up to factor 30. The biofunctionality was assessed in a microbiological assay. Surprisingly, the antimicrobial growth inhibition of the produced concentrate was even higher than in pure lactoferrin. The presented approach offers a strategy to convert an abundant but underutilized by-product into valuable products for human nutrition.

18.
Molecules ; 28(10)2023 May 17.
Article in English | MEDLINE | ID: mdl-37241878

ABSTRACT

Dragon's blood sap (DBS) obtained from the bark of Croton lechleri (Müll, Arg.) is a complex herbal remedy of pharmacological interest due to its high content in polyphenols, specifically proanthocyanidins. In this paper, electrospraying assisted by pressurized gas (EAPG) was first compared with freeze-drying to dry natural DBS. Secondly, EAPG was used for the first time to entrap natural DBS at room temperature into two different encapsulation matrices, i.e., whey protein concentrate (WPC) and zein (ZN), using different ratios of encapsulant material: bioactive compound, for instance 2:1 w/w and 1:1 w/w. The obtained particles were characterized in terms of morphology, total soluble polyphenolic content (TSP), antioxidant activity, and photo-oxidation stability during the 40 days of the experiment. Regarding the drying process, EAPG produced spherical particles with sizes of 11.38 ± 4.34 µm, whereas freeze-drying produced irregular particles with a broad particle size distribution. However, no significant differences were detected between DBS dried by EAPG or freeze-drying in TSP, antioxidant activity, and photo-oxidation stability, confirming that EAPG is a mild drying process suitable to dry sensitive bioactive compounds. Regarding the encapsulation process, the DBS encapsulated within the WPC produced smooth spherical microparticles, with average sizes of 11.28 ± 4.28 µm and 12.77 ± 4.54 µm for ratios 1:1 w/w and 2:1 w/w, respectively. The DBS was also encapsulated into ZN producing rough spherical microparticles, with average sizes of 6.37 ± 1.67 µm and 7.58 ± 2.54 µm for ratios 1:1 w/w and 2:1 w/w, respectively. The TSP was not affected during the encapsulation process. However, a slight reduction in antioxidant activity measured by DPPH was observed during encapsulation. An accelerated photo-oxidation test under ultraviolet light confirmed that the encapsulated DBS showed an increased oxidative stability in comparison with the non-encapsulated DBS, with the stability being enhanced for the ratio of 2:1 w/w. Among the encapsulating materials and according to the ATR-FTIR results, ZN showed increased protection against UV light. The obtained results demonstrate the potential of EAPG technology in the drying or encapsulation of sensitive natural bioactive compounds in a continuous process available at an industrial scale, which could be an alternative to freeze-drying.


Subject(s)
Antioxidants , Zein , Whey Proteins/chemistry
19.
J Sci Food Agric ; 103(11): 5242-5252, 2023 Aug 30.
Article in English | MEDLINE | ID: mdl-37029992

ABSTRACT

BACKGROUND: Protein-pectin conjugates, obtained through a controlled Maillard reaction in blends of precursors, are studied for their contribution to improving the emulsifying and thermal properties of proteins. The objective was to obtain a conjugate between whey protein concentrate (WPC) and non-conventional pectins extracted in acid (acid tomato pectin, ATP) and aqueous medium (water tomato pectin, WTP) from industrialized tomato residues (tomato waste, TW), characterize the conjugates and study their emulsion properties. The Maillard reaction was carried out at 60 °C and 75% relative humidity in blends with 2:1 proportions; 1:1 and 1:2 (mprotein :mpectin ) for 3, 6 and 12 days. Conjugates were compared concerning treated and untreated WPC. RESULTS: The WPC-ATP conjugate showed significant increases in color difference (ΔE). The electrophoresis profile of the conjugates showed diffuse bands of molecular weight between 37 and 250 kDa and a reduction in the intensity of bands characteristic of WPC (α-lactalbumin and ß-lactoglobulin). Thermal analysis showed an increase in the peak temperature and a reduction in the enthalpy change in protein denaturation, associated with the formation of conjugates. The infrared spectroscopy of the conjugates, in the amide III zone (1300-1100 cm-1 ), indicated an increase in the relative peak area associated with the unfolding and exhibition of the hydrophobic zones of the WPC fraction. The emulsions formulated with the conjugates showed a significant increase in the emulsifying stability index (ESI) (P < 0.05) concerning the treated and untreated WPC emulsions. CONCLUSION: The formation of conjugates increased the emulsifying properties and improved the thermal stability of WPC, showing an innovative and alternative food ingredient too. © 2023 Society of Chemical Industry.


Subject(s)
Pectins , Solanum lycopersicum , Whey Proteins/chemistry , Pectins/chemistry , Emulsions/chemistry , Adenosine Triphosphate
20.
Microorganisms ; 11(3)2023 Feb 22.
Article in English | MEDLINE | ID: mdl-36985131

ABSTRACT

The demand for healthy foods without artificial food additives is constantly increasing. Hence, natural food preservation methods using bioprotective cultures could be an alternative to chemical preservatives. Thus, the main purpose of this work was to screen the indigenous lactobacilli isolated from fermented cow milk for their safety and antifungal activity to select the safe strain with the strongest fungicidal properties for the development of bioprotective acid whey protein concentrate (AWPC) based fermentates and their coatings intended for fresh cheese quality maintenance. Therefore, 12 lactobacilli strains were isolated and identified from raw fermented cow milk as protective cultures. The safety of the stains was determined by applying antibiotic susceptibility, haemolytic and enzymatic evaluation. Only one strain, Lacticaseibacillus paracasei A11, met all safety requirements and demonstrated a broad spectrum of antifungal activity in vitro. The strain was cultivated in AWPC for 48 h and grew well (biomass yield 8 log10 cfu mL-1). L. paracasei A11 AWPC fermentate was used as a vehicle for protective culture in the development of pectin-AWPC-based edible coating. Both the fermentate and coating were tested for their antimicrobial properties on fresh acid-curd cheese. Coating with L. paracasei A11 strain reduced yeast and mould counts by 1.0-1.5 log10 cfu mL-1 (p ≤ 0.001) during cheese storage (14 days), simultaneously preserving its flavour and prolonging the shelf life for six days.

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