scholarly journals Development and Characterization of Whey Protein-Based Nano-Delivery Systems: A Review

Molecules ◽  
2019 ◽  
Vol 24 (18) ◽  
pp. 3254 ◽  
Author(s):  
Ho-Kyung Ha ◽  
Scott Rankin ◽  
Mee-Ryung Lee ◽  
Won-Jae Lee
Keyword(s):  
Physicochemical Properties ◽  
Whey Protein ◽  
Whey Proteins ◽  
Milk Proteins ◽  
Delivery Systems ◽  
Potential Health ◽  
Factors Affecting ◽  
Barrier Effects ◽  
Food Applications ◽  
Low Toxicity

Various bioactive compounds (BCs) often possess poor stability and bioavailability, which makes it difficult for them to exert their potential health benefits. These limitations can be countered by the use of nano-delivery systems (NDSs), such as nanoparticles and nanoemulsions. NDSs can protect BCs against harsh environments during food processing and digestion, and thereby, could enhance the bioavailability of BCs. Although various NDSs have been successfully produced with both synthetic and natural materials, it is necessary to fulfill safety criteria in the delivery materials for food applications. Food-grade materials for the production of NDSs, such as milk proteins and carbohydrates, have received much attention due to their low toxicity, biodegradability, and biocompatibility. Among these, whey proteins—from whey, a byproduct of cheese manufacturing—have been considered as excellent delivery material because of their high nutritional value and various functional properties, such as binding capability to various compounds, gelation, emulsifying properties, and barrier effects. Since the functional and physicochemical properties of whey protein-based NDSs, including size and surface charge, can be key factors affecting the applications of NDSs in food, the objectives of this review are to discuss how manufacturing variables can modulate the functional and physicochemical properties of NDSs and bioavailability of encapsulated BCs to produce efficient NDSs for various BCs.

scholarly journals Novel Delivery Systems of Polyphenols and Their Potential Health Benefits

2021 ◽  
Vol 14 (10) ◽  
pp. 946
Author(s):  
Bianca Enaru ◽  
Sonia Socaci ◽  
Anca Farcas ◽  
Carmen Socaciu ◽  
Corina Danciu ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Environmental Factors ◽  
Active Compound ◽  
Drug Delivery Systems ◽  
Delivery Systems ◽  
Potential Health ◽  
Future Studies ◽  
Beneficial Effects ◽  
Low Toxicity ◽  
Novel Delivery Systems

Liposome-based delivery systems have been studied and used more frequently in recent years due to their advantages, such as low toxicity, specificity, and the ability to protect the encapsulated substance from environmental factors, which could otherwise degrade the active compound and reduce its effectiveness. Given these benefits, many researchers have encapsulated polyphenols in liposomes, thus increasing their bioavailability and stability. Similarly, polyphenols encapsulated in liposomes are known to produce more substantial effects on targeted cells than unencapsulated polyphenols, while having minimal cytotoxicity in healthy cells. Although polyphenols play a role in preventing many types of disease and generally have beneficial effects on health, we solely focused on their chemopreventive effects on cancer through liposomes in this review. Our goal was to summarize the applicability and efficacy of liposomes encapsulated with different classes of polyphenols on several types of cancer, thus opening the opportunity for future studies based on these drug delivery systems.

scholarly journals Whey protein-derived biomaterials and their use as bioencapsulation and delivery systems

2003 ◽  
Vol 57 (12) ◽  
pp. 617-621 ◽  
Author(s):  
Muriel Subirade ◽  
Gabriel Remondetto ◽  
Lucie Beaulieu
Keyword(s):  
Food Systems ◽  
Serum Proteins ◽  
Whey Proteins ◽  
Health Benefits ◽  
Delivery Systems ◽  
Potential Health ◽  
Nutraceutical Compounds ◽  
Risk Of Disease ◽  
Physiological Benefits ◽  
Food Processes

The emergence of bioactive food compounds (nutraceutical compounds) with health benefits provides an excellent opportunity for improving public health. The incorporation of bioactive compounds into food systems is therefore of great interest to researchers in their efforts to develop innovative functional foods that may have physiological benefits or reduce the risk of disease beyond basic nutritional functions. However, the effectiveness of these products in preventing diseases relies on preserving the bioavailability of their active ingredients. This represents undoubtedly a great challenge since these molecules are generally sensitive to environmental conditions encountered in food processes (i.e., temperature oxygen, and light) or in the gastrointestinal tract (i.e., pH, enzymes presence of other nutrients), which limit their activity and potential health benefits. However, bio- and microencapsulation can be used to overcome these limitations. Whey proteins, also known as the serum proteins of milk, are widely used in food products, because of their high nutritional value and their ability to form gels, emulsions, or foams. The aim of this article is to provide information on the different types of materials obtained from whey proteins and to examine their use as bioencapsulation and delivery systems.

Influence of whey and purified whey proteins on neutrophil functions in sheep

1997 ◽  
Vol 64 (2) ◽  
pp. 281-288 ◽  
Author(s):  
CHUN W. WONG ◽  
AI H. LIU ◽  
GEOFFREY O. REGESTER ◽  
GEOFFREY L. FRANCIS ◽  
DENNIS L. WATSON
Keyword(s):  
Whey Protein ◽  
Inflammatory Responses ◽  
Whey Proteins ◽  
Milk Proteins ◽  
Superoxide Production ◽  
Whey Protein Concentrate ◽  
Dependent Manner ◽  
Protein Concentrate ◽  
Milk Whey

The effects of ruminant whey and its purified fractions on neutrophil chemotaxis and superoxide production in sheep were studied. Both colostral whey and milk whey were found to inhibit chemotaxis regardless of whether they were autologous or homologous, but the inhibitory effects were abolished by washing neutrophils with culture medium before their use in the chemotaxis assay. Colostral whey and milk whey also inhibited the chemotactic activity of zymosan-activated serum. Whey fractions of various degrees of purity such as lactoferrin, lacto-peroxidase, lactoferrin–lactoperoxidase, α-lactalbumin, bovine serum albumin and whey protein concentrate were then studied. While none of these proteins showed any effects on chemotaxis, lactoferrin–lactoperoxidase and whey protein concentrate were found to have an enhancing effect on superoxide production in a dose-dependent manner. Our results provide information on the modulatory role of ruminant milk proteins in inflammatory responses and warrant future investigation.

Factors affecting the thermostability of β-galactosidase (Streptococcus salivarius subsp. thermophilus) in milk: a quantitative study

1989 ◽  
Vol 56 (5) ◽  
pp. 785-792 ◽  
Author(s):  
Byeong-Seon Chang ◽  
Raymond R. Mahoney
Keyword(s):  
Phosphate Buffer ◽  
Enzyme Stability ◽  
Divalent Cations ◽  
Whey Proteins ◽  
Milk Proteins ◽  
Enzyme Concentration ◽  
Streptococcus Salivarius ◽  
Factors Affecting ◽  
Micellar Casein ◽  
Acting In Concert

SummaryEnhanced stability of β-galactosidase (Streptococcus salivarius subsp. thermophilus) in milk is due to several milk components acting in concert. Milk salts stabilized the enzyme 3-fold compared to phosphate buffer. K+ was a better stabilizer than Na+. Omission of divalent cations, especially Mg2+, caused a marked drop in stability. Lactose stabilized enzyme stored in the frozen state but destabilized enzyme stored unfrozen. Caseinate stabilized the enzyme 8-fold in phosphate buffer but it stabilized 144-fold in the presence of lactose. In the presence of milk proteins, lactose was 25 times as effective as galactose and 100 times as effective as glucose at promoting stability; sucrose slightly destabilized the enzyme. Stability rose with increasing lactose concentration but declined with increasing enzyme concentration. In milk, soluble casein was the primary stabilizer; whey proteins and peptides had much less effect. Micellar casein had no effect on stability.

scholarly journals Microstructure and Physicochemical Properties of Light Ice Cream: Effects of Extruded Microparticulated Whey Proteins and Process Design

Foods ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1433
Author(s):  
M Kamal Hossain ◽  
Miroslav Petrov ◽  
Oliver Hensel ◽  
Mamadou Diakité
Keyword(s):  
Shear Rate ◽  
Physicochemical Properties ◽  
Whey Protein ◽  
Process Design ◽  
Whey Proteins ◽  
Ice Cream ◽  
Melting Behavior ◽  
The Other ◽  
Fat Replacers ◽  
Other Hand

This study aimed to understand the influence of extruded microparticulated whey proteins (eMWPs) and process design in light ice cream processing by evaluating the microstructure and physicochemical properties. The inulin (T1), a commercial microparticulated whey protein (MWP) called simplesse (T2), a combination (T3), as well as eMWPs (as 50% volume of total particles): d50 < 3 µm (T4), and d50 > 5 µm (T5) were used as fat replacers. The first process design was pasteurization with subsequent homogenization (PH). The second process was homogenization with subsequent pasteurization (HP) for the production of ice cream (control, 12% fat, w/w; T1 to T5, 6% fat, w/w). The overrun of light ice cream treatments of PH was around 50%, except for T4 (61.82%), which was significantly higher (p < 0.01). On the other hand, the overrun of HP was around 40% for all treatments except T1. In both the PH and HP groups, the color intensities of treatments were statistically significant (p < 0.001). The melting behavior of light ice cream was also significantly different. The viscosity of all treatments was significant (p < 0.05) at a shear rate of 64.54 (1/s) for both cases of process design. A similar firmness in both the PH and HP groups was observed; however, the products with eMWPs were firmer compared to other light ice creams.

scholarly journals Effect of Protein Genotypes on Physicochemical Properties and Protein Functionality of Bovine Milk: A Review

Foods ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 2409
Author(s):  
Nan Gai ◽  
Therese Uniacke-Lowe ◽  
Jonathan O’Regan ◽  
Hope Faulkner ◽  
Alan L. Kelly
Keyword(s):  
Physicochemical Properties ◽  
Genetic Variants ◽  
Whey Proteins ◽  
Bovine Milk ◽  
Milk Proteins ◽  
Heat Stability ◽  
Foaming Properties ◽  
Rennet Coagulation ◽  
Acid Gel ◽  
Β Lactoglobulin

Milk protein comprises caseins (CNs) and whey proteins, each of which has different genetic variants. Several studies have reported the frequencies of these genetic variants and the effects of variants on milk physicochemical properties and functionality. For example, the C variant and the BC haplotype of αS1-casein (αS1-CN), β-casein (β-CN) B and A1 variants, and κ-casein (κ-CN) B variant, are favourable for rennet coagulation, as well as the B variant of β-lactoglobulin (β-lg). κ-CN is reported to be the only protein influencing acid gel formation, with the AA variant contributing to a firmer acid curd. For heat stability, κ-CN B variant improves the heat resistance of milk at natural pH, and the order of heat stability between phenotypes is BB > AB > AA. The A2 variant of β-CN is more efficient in emulsion formation, but the emulsion stability is lower than the A1 and B variants. Foaming properties of milk with β-lg variant B are better than A, but the differences between β-CN A1 and A2 variants are controversial. Genetic variants of milk proteins also influence milk yield, composition, quality and processability; thus, study of such relationships offers guidance for the selection of targeted genetic variants.

scholarly journals Hardness of high protein nutrition bars based on milk protein concentrates:a review

2020 ◽  
Vol 10 (1) ◽  
pp. 4914-4921
Keyword(s):  
Whey Protein ◽  
Milk Protein ◽  
Milk Proteins ◽  
High Protein ◽  
Native Form ◽  
Protein Sources ◽  
Protein Nutrition ◽  
Food Applications ◽  
Different Origins ◽  
Multifunctional Properties

High protein nutrition (HPN) bars are gaining increased global popularity as convenient and high nutritious food products. Proteins of different origins have been used singly or in combinations in HPN but milk proteins (whey protein products, casein and caseinates) remain the favorable proteins used in HPN formulations. Milk protein concentrates (MPC) of different protein contents are new milk protein ingredients of multifunctional properties for diversified food applications. They contain both casein and whey protein in their native form and ratio found in milk. The use of high protein MPCs in nutrition bars is one of the promising applications for these products. HPN based on different protein sources develops hardness during storage particularly at high temperatures but more pronounced hardness develops on the use of MPCs. Several approaches have been suggested to overcome this problem through modification of MPCs. This review presents an overview ofthe HPN bar hardness mechanisms and MPC modifications to combat this problem.

scholarly journals Whey Proteins as a Potential Co-Surfactant with Aesculus hippocastanum L. as a Stabilizer in Nanoemulsions Derived from Hempseed Oil

Molecules ◽  
2021 ◽  
Vol 26 (19) ◽  
pp. 5856
Author(s):  
Wojciech Smułek ◽  
Przemysław Siejak ◽  
Farahnaz Fathordoobady ◽  
Łukasz Masewicz ◽  
Yigong Guo ◽  
...  
Keyword(s):  
Droplet Size ◽  
Whey Proteins ◽  
Health Benefits ◽  
Droplet Size Distribution ◽  
Protein Isolate ◽  
Aesculus Hippocastanum ◽  
Potential Health ◽  
Factors Affecting ◽  
Natural Surfactants

The use of natural surfactants including plant extracts, plant hydrocolloids and proteins in nanoemulsion systems has received commercial interest due to demonstrated safety of use and potential health benefits of plant products. In this study, a whey protein isolate (WPI) from a byproduct of cheese production was used to stabilize a nanoemulsion formulation that contained hempseed oil and the Aesculus hippocastanum L. extract (AHE). A Box–Behnken experimental design was used to set the formulation criteria and the optimal nanoemulsion conditions, used subsequently in follow-up experiments that measured specifically emulsion droplet size distribution, stability tests and visual quality. Regression analysis showed that the concentration of HSO and the interaction between HSO and the WPI were the most significant factors affecting the emulsion polydispersity index and droplet size (nm) (p < 0.05). Rheological tests, Fourier transform infrared spectroscopy (FTIR) analysis and L*a*b* color parameters were also taken to characterize the physicochemical properties of the emulsions. Emulsion systems with a higher concentration of the AHE had a potential metabolic activity up to 84% in a microbiological assay. It can be concluded from our results that the nanoemulsion system described herein is a safe and stable formulation with potential biological activity and health benefits that complement its use in the food industry.

scholarly journals Reduction in the antigenicity of whey proteins by heat treatment: a possible strategy for producing a hypoallergenic infant milk formula

1984 ◽  
Vol 51 (1) ◽  
pp. 29-36 ◽  
Author(s):  
L. M. J. Heppell ◽  
A. J. Cant ◽  
P. J. Kilshaw
Keyword(s):  
Heat Treatment ◽  
Whey Protein ◽  
Antibody Production ◽  
Guinea Pigs ◽  
Whey Proteins ◽  
Milk Proteins ◽  
Heat Denaturation ◽  
Milk Formula ◽  
Milk Whey ◽  
Β Lactoglobulin

1. Residual antigenic protein in heat-denatured cow's milk whey and in two commercial infant milk formulas was determined using enzyme-linked immunosorbent assays specific for β-lactoglobulin, α-lactalbumin, bovine serum albumin, bovine IgG1 and α-casein. This immunochemical assessment of antigenicity was related to the capacity of the preparations to sensitize immunologically when fed to guinea-pigs for 2 weeks. Antibody production was measured and the susceptibility of the animals to systemic anaphylaxis was assessed by injecting them intravenously with heated or unheated milk proteins.2. Whey protein that had been heated at 100° or 115° for 30 min was extensively denatured and, in contrast to pasteurized whey, failed to sensitize guinea-pigs for anaphylaxis. Antibody production was undetected or very low. The proteins in SMA powder and SMA Gold Cap liquid concentrate were less denatured and animals given these formulas prepared according to the maker's instructions produced relatively high levels of antibodies to β-lactoglobulin and α-casein and a majority developed anaphylaxis when injected intravenously with these products.3. As well as failing to sensitize, whey that had received severe heat treatment did not, in most cases, elicit anaphylaxis when injected into animals that had been sensitized with unheated milk.4. Discrimination between antibodies of the IgG1 and IgG2 subclasses specific for β-lactoglobulin showed that IgG1, the principal anaphylactic antibody in guinea-pigs, was preferentially depressed in animals drinking heat-denatured milk preparations.5. The results suggest that heat denaturation of whey protein may be a logical and simple strategy for producing a hypoallergenic baby milk. Nevertheless, the value of experiments in guinea-pigs for predicting results in man is uncertain and the proposal awaits assessment in clinical trials.

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