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PubMed1985

Physiological and pathological factors influencing bovine alpha-lactalbumin and beta-lactoglobulin concentrations in milk.

Bovine alpha-lactalbumin and beta-lactoglobulin concentrations were determined by radial immunodiffusion in 354 milk samples from uninfected and 98 samples from infected quarters from 42 Holstein-Friesian cows taken at 30, 150, and 270 days of lactation. alpha-Lactalbumin and beta-lactoglobulin concentrations were not affected by quarter location. The alpha-lactalbumin decreased at the end of lactation and in samples collected beyond second lactation. The beta-lactoglobulin concentration increased with stage of lactation. There was a positive correlation between alpha-lactalbumin and beta lactoglobulin (r = .12). Milk from uninfected quarters had mean alpha-lactalbumin and beta-lactoglobulin concentrations of 1.47 and 4.6 mg/ml, respectively. Milk from quarters infected by major pathogens or Corynebacterium bovis had less alpha-lactalbumin. Milk from quarters infected by minor pathogens had less beta-lactoglobulin. There was a negative correlation between alpha-lactalbumin concentration and somatic cell count (r = .31), which was amplified by infection status of quarters. No correlation was noted between somatic cell count and beta-lactoglobulin concentration when considered over the whole sampling period, but the correlation became negative in quarters infected by major pathogens.

Animals↗

PubMed1993

Inhibition of plasmin by beta-lactoglobulin using casein and a synthetic substrate.

Bovine plasmin (EC 3.4.21.7) activity was measured on H-D-valyl-L-leucyl-L-lysyl-4-nitroanilide and acid casein in the presence of native and heat-denatured beta-lactoglobulin (denatured at 100 degrees C for 15 min before being mixed with plasmin solutions). Native or denatured beta-lactoglobulin was then heated with plasmin at 60 degrees C for 15 min. Enzyme activity again was estimated after this mild heat treatment. Native and denatured beta-lactoglobulin inhibited the action of plasmin on H-D-valyl-L-leucyl-L-lysyl-4-nitroanilide and casein. The mild heat treatment (60 degrees C for 15 min) caused stronger inhibition of the activity of plasmin against casein and the synthetic substrate. For H-D-valyl-L-leucyl-L-lysyl-4-nitroanilide, inhibition was competitive in unheated mixtures, but heating beta-lactoglobulin with plasmin changed inhibition type to mixed. This change suggests a heat-dependent interaction between plasmin and beta-lactoglobulin. Native beta-lactoglobulin was more inhibitory of plasmin's action against casein than was denatured beta-lactoglobulin. The converse was observed when plasmin activity was measured with the synthetic substrate.

Animals↗

PubMed1995

Interaction of beta-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: a review.

beta-Lactoglobulin is the major whey protein in the milk of ruminants and some nonruminants, such as pigs and horses. Although beta-lactoglobulin was first isolated 60 yr ago, no function has been definitely ascribed to beta-lactoglobulin. Recent x-ray crystallographic studies have advanced knowledge of the structure of beta-lactoglobulin, which is homologous with that of retinol-binding protein and lipocalycins; the function of these proteins seems to be participation in the transport of small hydrophobic substances. By analogy, this protein has been suggested as having a role as a transporter of fatty acids and retinol. This review reassesses the function of beta-lactoglobulin in light of the large amount of information that has accrued in the last few years. In particular, this review concentrates upon studies of the binding of retinol and fatty acids to beta-lactoglobulin, including the binding constants and number of binding sites, the location of the binding sites, and the influence of chemical modifications in the interaction of the protein with both ligands. This study also describes studies of the influence of beta-lactoglobulin on several biological processes that may be relevant to the possible biological role of this protein.

Animals↗

PubMed1990

Synthesis and evolution of concentration of beta-lactoglobulin and alpha-lactalbumin from cow and sheep colostrum and milk throughout early lactation.

Synthesis of beta-lactoglobulin and alpha-lactalbumin by explants of ovine mammary gland and evolution of concentration of these proteins in cow and sheep colostrum and milk throughout early lactation have been studied. The evolution of both proteins was similar in cow and sheep species. The highest concentration was found in the first milking (19 and 2 mg/ml for beta-lactoglobulin and alpha-lactalbumin, respectively). Then, levels of beta-lactoglobulin decreased sharply and those of alpha-lactalbumin slowly during the first days of lactation, reaching stable values during the second week postpartum (4 and 1.5 mg/ml). The concentration ratio beta-lactoglobulin/alpha-lactalbumin was four times greater in colostrum than in mature milk. On the other hand, synthesis of these proteins represented about 25-30% of the synthesized total soluble proteins. The synthesis ratio beta-lactoglobulin/alpha-lactalbumin in explants obtained at 12 and 30 hours postpartum was found to be 3.5 and 1.7. These results indicate that the synthesis and secretion of beta-lactoglobulin are comparatively greater than those of alpha-lactalbumin during colostral period, suggesting that beta-lactoglobulin could have some specific function during this period.

Animals↗

PubMedDate not supplied

[Possibility of fortifying milk nutrient mixtures for children with lactoglobulin against E. coli and Proteus].

Sweet milk nutrient mixtures, biologically active additives (BAA) and lactic acid ferments, intended for child nutrition, were enriched with the immune preparation lactoglobulin against E. coli and Proteus. Serological and immunochemical investigations of hemagglutinating activity and other characteristics of lactoglobulin in the enriched milk mixtures and BAA evidenced that the preparation retained its full value during the technological process and in the period of storage. No signs of lactoglobulin degradation during the production of a test batch of the milk mixture and BAA were detected, and a high hemagglutinating activity with respect to enteropathogenic E. coli and Proteus was recorded. This permitted the author to recommend the lactoglobulin-enriched sweet mixtures for prevention of acute intestinal infections and dysbacteriosis in young children. The in vitro study of the lactoglobulin interaction with pure cultures of lactobacillus and bifidobacteria showed its inertness to eubacteria. Four strains studied retained their growth and acid-forming properties after combined incubation with lactoglobulin and did not inhibit its activity. A conclusion has been made on the possibility of enrichment of lactic acid products, intended for child nutrition, with lactoglobulin against E. coli and Proteus.

Animals↗

PubMed1995

Nitrogen movements in the upper jejunum lumen in humans fed low amounts of casein or beta-lactoglobulin.

OBJECTIVES AND METHODS: To compare the progression of milk proteins in the upper part of the digestive tract, gastro-jejunal nitrogen movements were studied in 6 healthy human volunteers after beta-lactoglobulin and casein ingestion. 400 mL of water (control), purified beta-lactoglobulin (20 g/L) or casein (20 g/L), each adjusted to 25 microCi with 14C-polyethylene glycol, were given per os. Samples were collected in the stomach and 20 cm below the Treitz ligament every 20 min for 2 hours and measured for volume, osmolarity, ions and nitrogen content. RESULTS: The jejunal flow rate peaked in the 0-20 min period following water and beta-lactoglobulin ingestion, and in the 20-40 min period after casein ingestion. The gastric half-emptying time (T1/2 min) of the liquid phase was significantly different (P < 0.05) for water (12.1 +/- 0.8), beta-lactoglobulin (14.5 +/- 3.3) and casein (26.5 +/- 9.3). Before ingestion of the test meals, the basal rate of nitrogen was 9.14 +/- 4.09 mmol/h in the jejunum. The total nitrogen content in the jejunum peaked significantly in the 0-20 min period after beta-lactoglobulin ingestion and the 20-40 min period after casein ingestion. The apparent gastro-jejunal protein absorption values were 63% for casein and 66% for beta-lactoglobulin in the 120 min period. CONCLUSIONS: These results show that beta-lactoglobulin and casein behave differently in the upper part of the digestive tract due to different gastric emptying rates.

Adult↗

PubMed1993

Probing the fatty acid binding site of beta-lactoglobulins.

The interactions of fatty acids with porcine and bovine beta-lactoglobulins were measured using tryptophan fluorescence enhancement. In the case of bovine beta-lactoglobulin, the apparent binding constants for most of the saturated and unsaturated fatty acids were in the range of 10(-7) M at neutral pH. Bovine beta-lactoglobulin displays only one high affinity binding site for palmitate with an apparent dissociation constant of 1 x 10(-7) M. The strength of the binding was decreasing in the following way: palmitate > stearate > myristate > arachidonate > laurate. Caprylic and capric acids are not bound at all. The affinity of beta-lactoglobulin for palmitate decreased as the pH of the incubation medium was lowered and BLG/palmitate complex was not observed at pH's lower than 4.5. Surprisingly, chemically modified bovine beta-lactoglobulin and porcine beta-lactoglobulin did not bind fatty acids in the applied conditions.

Amino Acid Sequence↗

PubMed1992

Effect of beta-lactoglobulin on the activity of pregastric lipase. A possible role for this protein in ruminant milk.

The interaction of bovine beta-lactoglobulin with palmitic and oleic acids has been studied by a partition equilibrium method. Bovine beta-lactoglobulin displays only one high affinity binding site for fatty acids whose association constants for palmitic and oleic acids are 4.2 x 10(6) and 2.3 x 10(6) M-1, respectively. However, other binding sites with low affinity are also present. The existence of one high affinity binding site is in accordance with the amount of fatty acids naturally bound to beta-lactoglobulin isolated from milk. The effect of beta-lactoglobulin on ruminant pregastric lipases from a pharyngeal extract has been assayed. The activity of pharyngeal lipase on a triglyceride emulsion is increased about 200%, 250% and 190% in the presence of 10 mg/ml, 20 mg/ml and 40 mg/ml of beta-lactoglobulin, respectively, the last concentration representing that found physiologically in colostrum. Albumin, another ligand-binding protein, increases the activity of this enzyme to a lesser extent and high levels tend to inhibit enzyme action. These results indicate that beta-lactoglobulin could participate in the digestion of milk lipids during the neonatal period by enhancing the activity of pregastric lipase through removal of the fatty acids that inhibit this enzyme.

Animals↗

PubMed1990

Beta-lactoglobulin binds retinol and protoporphyrin IX at two different binding sites.

Measurement of tryptophan fluorescence quenching and the excitation energy transfer from tryptophanyl residues to the bound ligand indicates that beta-lactoglobulin binds tightly to hemin and protoporphyrin IX in a ligand-to-protein stoichiometric ratio. The apparent dissociation constants of hemin-beta-lactoglobulin and protoporphyrin IX-beta-lactoglobulin complexes are 2.5 x 10(-7) M and 4 x 10(-7) M, respectively. The addition of beta-lactoglobulin (final concentration = 10 microM, phosphate buffer 50 mM, pH 7.1) to the solution containing retinol and protoporphyrin IX triggers an energy transfer between beta-lactoglobulin tryptophan and protoporphyrin IX as well as between retinol and protoporphyrin IX. The efficiency of energy transfer depends on the distance between the donor (retinol) and the acceptor (protoporphyrin IX). Using the Förster theory, a retinolprotoporphyrin IX distance of 25 A was calculated. These results indicate that retinol and protoporphyrin IX are bound to the beta-lactoglobulin monomer at two different sites.

Animals↗

PubMed1991

Time-dependent polymerization of beta-lactoglobulin through disulphide bonds at the oil-water interface in emulsions.

Time-dependent intermolecular sulphydryl-disulphide interchange involving beta-lactoglobulin adsorbed at the oil-water interface in n-tetradecane-in-water emulsions (10 wt% oil, 0.5 wt% protein, pH 7.0) has been investigated using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). While only monomers are detected in the adsorbed protein immediately after emulsion formation with pure beta-lactoglobulin, on storing the emulsion the amount of polymerized beta-lactoglobulin and the sizes of the oligomers are found to increase with time. There is no polymerization of adsorbed protein in emulsions made with pure alpha-lactalbumin after 72 h, or in emulsions made with beta-lactoglobulin in the presence of a reagent (N-ethylmaleimide) for modifying sulphydryl groups. Analysis by two-dimensional SDS-PAGE of adsorbed protein from aged emulsions made with a mixture of alpha-lactalbumin + beta-lactoglobulin shows some linking by disulphide bonds between alpha-lactalbumin and beta-lactoglobulin at the interface. Taken together with earlier time-dependent surface viscosity measurements, the results indicate the important role of free sulphydryl groups in the development of the high surface viscoelasticity of adsorbed globular proteins at the oil-water interface.

Adsorption↗

PubMed1991

Binding of retinoids and beta-carotene to beta-lactoglobulin. Influence of protein modifications.

The binding of retinol, retinyl acetate, retinoic acid and beta-carotene to native, esterified and alkylated beta-lactoglobulin was followed by quenching of tryptophan fluorescence. Three studied retinoids bind to native or modified beta-lactoglobulin in 1:1 molar ratios, with apparent dissociation constants in the range of 10(-8) M. The maximum tryptophan fluorescence quenching of unmodified beta-lactoglobulin by beta-carotene is observed at the ligand/protein ratio of 1:2. Esterification and alkylation of beta-lactoglobulin shift the ratio of beta-carotene/protein to 1:1. In all the cases, except for retinoic acid binding to N-ethyllysyl-BLG, the performed chemical modifications of beta-lactoglobulin enhance protein binding affinity. Measured apparent dissociation constants of beta-carotene complexes with native and modified beta-lactoglobulin are an order of magnitude lower from binding constants of other studied retinoids.

Carotenoids↗

PubMed2005

Cooperative alpha-helix formation of beta-lactoglobulin induced by sodium n-alkyl sulfates.

It is generally assumed that folding intermediates contain partially formed native-like secondary structures. However, if we consider the fact that the conformational stability of the intermediate state is simpler than that of the native state, it would be expected that the secondary structures in a folding intermediate would not necessarily be similar to those of the native state. beta-Lactoglobulin is a predominantly beta-sheet protein, although it has a markedly high intrinsic preference for alpha-helical structure. The formation of non-native alpha-helical intermediate of beta-lactoglobulin was induced by n-alkyl sulfates including sodium octyl sulfate, SOS; sodium decyl sulfate, SDeS; sodium dodecyl sulfate, SDS; and sodium tetradecyl sulfate, STS at special condition. The effect of n-alkyl sulfates on the structure of native beta-lactoglobulin at pH 2 was utilized to investigate the contribution of hydrophobic interactions to the stability of non-native alpha-helical intermediate. The addition of various concentrations of n-alkyl sulfates to the native state of beta-lactoglobulin (pH 2) appears to support the stabilized form of non-native alpha-helical intermediate at pH 2. The m values of the intermediate state of beta-lactoglobulin by SOS, SDeS, SDS and STS showed substantial variation. The enhancement of m values as the stability criterion of non-native alpha-helical intermediate state corresponded with increasing chain length of the cited n-alkyl sulfates. The present results suggest that the folding reaction of beta-lactoglobulin follows a non-hierarchical mechanism and hydrophobic interactions play important roles in stabilizing the non-native alpha-helical intermediate state.

Alkylation↗

PubMed1999

Interaction mode specific reorganization of gel phase monoglyceride bilayers by beta-lactoglobulin.

The interaction between beta-lactoglobulin and sonicated aqueous dispersions of the gel phase forming monoglyceride monostearoylglycerol were studied using isothermal titration calorimetry, direct binding experiments, differential scanning calorimetry, leakage of a fluorescent dye and solid-state (31)P- and (2)H-NMR. In the absence of a charged amphiphile, monostearoylglycerol forms a precipitate. Under these conditions, no interaction with beta-lactoglobulin was observed. In the presence of the negatively charged amphiphile dicetylphosphate, the gel phase monostearoylglycerol formed stable and closed, probably unilamellar, vesicles with an average diameter of 465 nm. beta-Lactoglobulin interacts with these bilayer structures at pH 4, where the protein is positively charged, as well as at pH 7 where the protein is negatively charged. Under both conditions of pH, the binding affinity of beta-lactoglobulin is in the micromolar range as observed with ITC and the direct binding assay. At pH 4, two binding modes were found, one of which is determined with ITC while the direct binding assay determines the net result of both. The first binding mode is observed with ITC and is characterized by a large binding enthalpy, a decreased enthalpy of the MSG L(beta) to L(alpha) phase transition and leakage of a fluorescent dye. These characteristics are explained by a beta-lactoglobulin induced partial L(beta) to coagel phase transition that results from a specific electrostatic interaction between the protein and the charged amphiphile. This explanation is confirmed by solid-state (2)H-NMR using 1-monostearoylglycerol with a fully deuterated acyl chain. Upon interaction with beta-lactoglobulin, the isotropic signal in the (2)H-NMR spectrum of the monostearoylglycerol-dicetylphosphate mixture partially transforms into a broad anisotropic signal which could be assigned to coagel formation. The second binding mode probably results from an aspecific electrostatic attraction between the negatively charged bilayer and the positively charged protein and causes the precipitation of the dispersion. At pH 7, only the first binding mode is observed.

Animals↗

PubMed1998

Exposure to cow's milk during the first 3 months of life is associated with increased levels of IgG subclass antibodies to beta-lactoglobulin to 8 years.

BACKGROUND: Exposure to allergens early in life influences the development of allergen-specific immune responses. In animal models, the development of tolerance to proteins delivered to the gastrointestinal and the respiratory mucosa is influenced by age and genetic background. Late introduction of cow's milk in infants is associated with slower increase and lower peak IgG antibody responses to milk during early childhood, but the long-term effects have not been investigated, nor is the relation to atopic disease later in life clear. OBJECTIVE: The purpose of this study was to investigate the development of IgG subclass antibodies to beta-lactoglobulin in relation to early exposure to cow's milk, atopic heredity, and the development of atopic disease. METHODS: IgG subclass antibodies to beta-lactoglobulin were analyzed by ELISA at birth, at 6 and 18 months, and at 8 years in 96 children followed prospectively. RESULTS: The levels of IgG subclass antibodies to beta-lactoglobulin peaked in early childhood and then declined up to 8 years of age. Exposure to cow's milk during the first 3 months of life was associated with high IgG subclass antibody levels to beta-lactoglobulin up to 8 years, particularly in children with maternal atopy. Children with atopic symptoms and sensitivity to allergens often had high levels of IgG4 antibodies to beta-lactoglobulin at 8 years of age, even if they were not exposed to cow's milk during the first 3 months of life. Furthermore, atopic dermatitis was associated with high levels of IgG subclass antibodies to beta-lactoglobulin in early childhood. CONCLUSIONS: IgG subclass antibody levels to milk peak during early infancy, with particularly high levels in children with atopic dermatitis, and decline thereafter. Exposure to cow's milk during early infancy has long-lasting effects on the humoral antigen-specific responses, indicating less effective tolerance-inducing mechanisms in the intestinal mucosa during the first months of life.

Animals↗

PubMed1997

Development of IgG1 and IgG4 antibodies against beta-lactoglobulin and ovalbumin in healthy and atopic children.

BACKGROUND: The IgG responses to food antigens are preferentially restricted to the IgG1 and IgG4 subclasses. Increased levels of IgG1 and IgG4 antibodies against food allergens have been reported in girls and adults with current atopic eczema. OBJECTIVE: To study the relation between the levels of IgG1 and IgG4 antibodies against beta-lactoglobulin and ovalbumin and the development of atopic disease. MATERIAL AND METHODS: Atopic symptoms were recorded in 36 girls from birth to 7 years of age. Blood samples were taken at 3 and 8 months and at 2, 4, and 7 years. IgG1 and IgG4 antibodies were measured by ELISA. RESULTS: Anti-beta-lactoglobulin IgG1 was detected at all ages, peaking at 8 months. Anti-beta-lactoglobulin IgG4 antibodies were detected in 18 to 29 girls at different ages and the antibody levels peaked at 2 years. The levels of anti-beta-lactoglobulin IgG1 were lower in atopic, as compared with healthy individuals at 4 and 7 years (P < .01 and P < .05) and lower anti-beta-lactoglobulin IgG4 antibody levels were found in atopic individuals (P < .05) at 4 years. Anti-ovalbumin IgG1 antibodies were detected in 3/35 girls at 3 months and in 16/35 to 26/35 girls later in life. The number of positive samples and antibody levels peaked at 2 years. Anti-ovalbumin IgG4 positive samples increased from 4/33 at 8 months to 30/32 at 7 years. The levels increased up to 2 years and then remained stable. The anti-ovalbumin IgG1 antibody levels were lower in atopic girls at 4 years (P < .05), while the anti-ovalbumin IgG4 antibody levels were similar at all ages. CONCLUSION: An early IgG1 response and later appearing IgG4 antibodies to the two food antigens beta-lactoglobulin and ovalbumin are common during the first years of life. The levels were similar in the nonatopic and the atopic girls up to four years; then they tended to be lower in the first group.

Adult↗

PubMed2000

Purification of goat beta-lactoglobulin from whey by an ultrafiltration membrane enzymic reactor.

This paper presents a novel contribution to the purification of goat beta-lactoglobulin by using an ultrafiltration membrane enzymic reactor. The basis of the purification process was the enzymic hydrolysis of contaminating proteins, alpha-lactalbumin and traces of serum albumin, by pepsin at 40 degrees C and pH 2, conditions under which beta-lactoglobulin is resistant to peptic digestion. Simultaneously, beta-lactoglobulin and peptides were separated by ultrafiltration. beta-Lactoglobulin was retained in the reactor while peptides generated by hydrolysis from alpha-lactalbumin and serum albumin permeated through the membrane. The process was made continuous by the addition of fresh whey to replace the lost permeate. Three mineral membranes with 10, 30 and 50 kDa molecular mass cut-off were tested and the 30 kDa membrane was selected for the continuous process. The simultaneous purification and concentration of beta-lactoglobulin from clarified goats' whey was achieved in a single step. The ultrafiltration membrane enzymic reactor could treat eight reactor volumes of clarified whey. The recovery of beta-lactoglobulin was 74%, its purity was 84% and its concentration 6.6-fold that in the initial clarified whey.

Animals↗

PubMed2000

Riboflavin-sensitized photochemical changes in beta-lactoglobulin in an aqueous buffer solution as affected by ascorbic acid.

The effects of ascorbic acid on the riboflavin-sensitized photochemical changes in beta-lactoglobulin in an aqueous buffer solution as determined by high performance gel permeation liquid chromatography (HPGPLC), insoluble protein content, and individual amino acid content during fluorescent light illumination were studied. The riboflavin-sensitized photochemical degradation of beta-lactoglobulin was effectively inhibited by ascorbic acid, and its inhibitory effectiveness was concentration dependent. The 0.1% ascorbic acid treatment showed 74.4% inhibition of beta-lactoglobulin degradation as determined by a HPGPLC during 6 h light illumination. Insolubility of beta-lactoglobulin in a buffer solution during light illumination was also effectively decreased by ascorbic acid treatment. The riboflavin-sensitized photochemical reduction of cysteine, histidine, lysine, methionine, and tryptophan in beta-lactoglobulin was high during 6 h fluorescent light illumination. The 0.1% ascorbic acid treatment exhibited 20.8% inhibition of total amino acid degradation in beta-lactoglobulin during 6 h light illumination, showing strong inhibitory activity against the degradation of arginine, aspartic acid, cystein, glycine, histidine, phenylalanine, proline, serine, and tryptophan.

Ascorbic Acid↗

PubMed2007

Microstructure of beta-lactoglobulin/pectin coacervates studied by small-angle neutron scattering.

Small-angle neutron scattering (SANS) has been used to investigate the microstructure of beta-lactoglobulin/pectin coacervates prepared by different initial protein/polysaccharide weight ratio (r), sodium chloride concentration (C(NaCl)), and pectin charge density. The higher r and higher pectin charge density lead to higher scattering intensity at small q range (0.007 Angstrom(-1) < q < 0.02 Angstrom(-1)), suggesting that the charges of pectin chains are screened significantly by the binding of oppositely charged protein molecules, leading to a tighter aggregation of pectin chains. On the other hand, the appearance of a shoulder peak at intermediate q range (0.04 Angstrom(-1) < q < 0.2 Angstrom(-1)) is used to interpret the formation of protein domains in beta-lactoglobulin/pectin coacervates. At C(NaCl) = 0.1 M, the coacervate of beta-lactoglobulin and pectin A does not show a shoulder peak at intermediate q range at r = 10:1, suggesting that protein molecules are separately bound on pectin chains. However, a shoulder peak appears at intermediate q range at r = 20:1 and 30:1, and the average protein domain size estimated from the shoulder peak position is 7.2 and 8.5 nm, respectively, for these two coacervates. When C(NaCl) increases from 0.05 to 0.2 M, the shoulder peak shifts toward smaller q and becomes broader, indicating that the addition of a higher amount of salt leads to a more heterogeneous coacervate structure. Pectin B with a lower linear charge density favors the formation of larger protein domains. The formation of protein domains in beta-lactoglobulin/pectin coacervates is partially ascribed to the self-aggregation of beta-lactoglobulin molecules. Two kinds of microstructures of beta-lactoglobulin/pectin coacervates with and without observable protein domains have been proposed.

Algorithms↗