• Food Science of Animal Resources
• /
• v.30 no.4
• /
• pp.575-581
• /
• 2010

This investigation was aimed at developing a ready-to-reconstitute beverage by utilizing probiotics and whey protein hydrolysates carrying bioactive peptides. Cheddar cheese whey was ultrafiltered. The 18% protein retentate was subjected to protein hydrolysis using Neutrase. The hydrolyzed retentate was further condensed to 35% total solids and spray-dried at $75^{\circ}C$ outlet air temperature. Different levels of sugar, citric acid and stabilizer were blended for spray-dried hydrolysates. Spray-dried hydrolysate was further inoculated with different levels of probiotics grown in a whey medium and dried in fluidized-bed drier at $40^{\circ}C$ to obtain a ready-to-reconstitute beverage. Hydrolysis was greatest at an enzyme:substrate ratio of 1:25 for 3 h. Spray-dried hydrolysate reconstituted to 1% protein and blended with 15% sugar, 0.2% citric acid and 0.15% xantham gum resulted in a superior product with no sedimentation. Accordingly, sugar, citric acid and xanthum gum were dry-blended with spray-dried hydrolysates. Bifidobacterium bifidum and Lactobacillus acidophilus that was grown separately in a whey medium, blended to produce 2% spray-dried hydrolysate and dried as described above resulted in a readyto-reconstitute beverage mix. The fluidized dried product typically exhibited a probiotic count of $10^8$colony forming units (CFU)/g. However, blending of probiotic to the retentate and direct spray-drying precipitously reduced the probiotic count to $10^4$ CFU/g of powder.

• Food Science of Animal Resources
• /
• v.23 no.1
• /
• pp.63-69
• /
• 2003

This experiment was carried out to study changes in solubility and emulsifying properties of whey protein. Whey protein hydrolysates were obtained from tryptic hydrolysis of whey protein concentrate at pH 8.0 and 37$^{\circ}C$ for 6 hours. Emulsifying activity of whey protein hydrolysate was highest at 4 hours of hydroysis and at 5.50% of DH. During hydrolysis of whey protein concentrate with trypsin, ${\alpha}$-lactalbumin was not easily broken down. But ${\beta}$-lactoglobulin was hydrolysed rapidly from the early stage of hydrolysis, producing several low molecular weight peptides, which have to participate in increasing emusifying activity. The solulbility of hydyolysates tended to increase depending on hydrolysis time; however, there was a gradual decrease after 5 hours. The hydrolysate had a minimum solubility near the isoelectric point range (pH 4∼5). The more hydrolysed the whey protein concentrates, the more soluble they are near the pl. They aye also more soluble above pH 6. Emulsifying activity of hydrolysates showed similar results to solubility. Creaming stability gradually increased when hydrolysis increased, increasing rapidly above pH 8 after 4 hours of hydrolysis.

• Food Science of Animal Resources
• /
• v.38 no.4
• /
• pp.780-793
• /
• 2018

This study was conducted to compare the anti-allergic effects of a whey protein concentrate (WPC) and WPC hydrolysate. WPC hydrolysate was prepared using enzymatic digestion for 8 h with trypsin and ${\alpha}$-chymotrypsin, after which it was freeze-dried. The allergic parameters assessed in rat basophilic leukemia (RBL)-2H3 cells were degranulation and release of ${\beta}$-hexosaminidase, release of tumor necrosis factor $(TNF)-{\alpha}$, and changes in the expression of $IL-1{\beta}$, IL-4, and IL-10 by real time polymerase chain reaction (PCR). During preparation of the WPC hydrolysate, hydrolysis increased rapidly from 0 to 10 min and then gradually increased slowly from 1 h onwards, achieving a final degree of hydrolysis of 78.50%. The SDS-PAGE analysis revealed a reduction in the intensity of several protein bands in the WPC hydrolysate compared to the WPC. IgE-induced ${\beta}$-hexosaminidase release from RBL-2H3 cells was decreased to a higher degree following treatment with the hydrolysate compared to WPC treatment. W500 ($500{\mu}g/mL$ WPC) showed the least inhibition of ${\beta}$-hexosaminidase release, but there was no significant difference between W500 and W1000 ($1,000{\mu}g/mL$) (p<0.05). H1000 ($1,000{\mu}g/mL$ WPC hydrolysate) inhibited ${\beta}$-hexosaminidase release by 39%. Compared to the control, treatment with H1000 decreased $TNF-{\alpha}$ secretion to 11.87 pg/mL. The gene expression levels of IL-1${\beta}$, IL-4, and IL-13 were all significantly decreased in hydrolysate (p<0.05). In the case of $IL-1{\beta}$ and IL-4, the expression levels in W1000 treated cells were decreased by 73.67% and 65%, respectively, and that of IL-13 was decreased by 66.43% compared to the control.

• Food Science of Animal Resources
• /
• v.31 no.6
• /
• pp.886-892
• /
• 2011

This study investigated the ACE-inhibitory effect of yogurt beverage fortified with hydrolysates as well as the suitability of hydrolysates as a nutraceutical additive to yogurt beverage. Three whey protein hydrolysates hydrolyzed by alcalase, protamex, and trypsin were each added to yogurt beverage at concentrations of 1.25, 2.5, and 5 mg/mL. Yogurt beverage fortified with 2.5 mg/mL of hydrolysates had 61-69% ACE-inhibitory activity, whereas yogurt beverage fortified with 5 mg/mL of hydrolysates showed 74% ACE-inhibitory activity. There were no significant differences in ACE-inhibitory activity between the alcalase or protamex hydrolysates during storage; however, trypsin hydrolysate exhibited significant differences. On the other hand, physicochemical characteristics such as pH (3.47-3.77), titratable acidity (0.81-0.84%), colority, viable cell count, and sensory qualities were not significantly different among the tested yogurt beverage samples during storage. These results showed that yogurt beverage fortified with whey protein hydrolysates maintained antihypertensive activity and underwent no unfavorable changes in physicochemical characteristics regardless of enzyme type.

• Journal of Ginseng Research
• /
• v.46 no.2
• /
• pp.283-289
• /
• 2022

Background: Sarcopenia, defined as loss of muscle mass and strength with age, becomes a public health concern as the elderly population increases. This study aimed to determine whether the mixture of soluble whey protein hydrolysate (WPH) and Panax ginseng berry extract (GBE) has a synergetic effect on sarcopenia and, if so, to identify the relevant mechanisms and optimal mixing ratio. Methods: In the first experiment, C57BL/6 mice were hindlimb immobilized for one-week and then administered WPH 800 mg/kg, GBE 100 mg/kg, WPH 800 mg/kg+ GBE 100 mg/kg mixture, and Fructus Schisandrae extract (SFE) 200 mg/kg for two weeks. In the second experiment, experimental design was same, but mice were administered three different doses of WPH and GBE mixture (WPH 800 mg/kg+ GBE 100 mg/kg, WPH 800 mg/kg+ GBE 90 mg/kg, WPH 1000 mg/kg+ GBE 75 mg/kg). Results: In the first experiment, we confirmed the synergetic effect of WPH and GBE on muscle mass and identified that GBE was more effective on the protein synthesis side, and WPH tended to be slightly more effective for protein degradation. In the second experiment, among three different ratios, the WPH 800 mg/kg+ GBE 100 mg/kg was most effective for muscle mass and strength. The mixtures activated muscle protein synthesis via PI3K/Akt/mTORc1 pathway and inhibited muscle protein degradation via suppressing ubiquitin-proteasome system (UPS) and autophagy-lysosome system (ALS), and these effects were more GBE dose-dependent than WPH. Conclusion: The WPH and GBE mixture having a synergetic effect is a potential agent to prevent sarcopenia.

• Food Science of Animal Resources
• /
• v.35 no.3
• /
• pp.350-359
• /
• 2015

This review focuses on the enhanced functional characteristics of enzymatic hydrolysates of whey proteins (WPHs) in food applications compared to intact whey proteins (WPs). WPs are applied in foods as whey protein concentrates (WPCs), whey protein isolates (WPIs), and WPHs. WPs are byproducts of cheese production, used in a wide range of food applications due to their nutritional validity, functional activities, and cost effectiveness. Enzymatic hydrolysis yields improved functional and nutritional benefits in contrast to heat denaturation or native applications. WPHs improve solubility over a wide range of pH, create viscosity through water binding, and promote cohesion, adhesion, and elasticity. WPHs form stronger but more flexible edible films than WPC or WPI. WPHs enhance emulsification, bind fat, and facilitate whipping, compared to intact WPs. Extensive hydrolyzed WPHs with proper heat applications are the best emulsifiers and addition of polysaccharides improves the emulsification ability of WPHs. Also, WPHs improve the sensorial properties like color, flavor, and texture but impart a bitter taste in case where extensive hydrolysis (degree of hydrolysis greater than 8%). It is important to consider the type of enzyme, hydrolysis conditions, and WPHs production method based on the nature of food application.

• Journal of Dairy Science and Biotechnology
• /
• v.25 no.1
• /
• pp.1-7
• /
• 2007

A Whey-based medium was formulated with Lactobacillus brevis to investigate whether any functional peptides could derive from whey protein. The optimal concentrations of the ingredients of the medium for the growth of Lactobacillus were determined as 2% whey protein concentrate and 1% glucose and 0.5% yeast extracts. The growth of Lb. brevis was improved with the supplementation of yeast extracts than glucose. The viable cells counts of Lb. brevis reached to 2.0 × 10$^8$CFU/mL in the whey-based medium. The whey protein hydrolysates recovered from the supernatant after centrifugation at 10,000 x g for 10min induced strong inhibitory activity against ACE. When the whey protein hydrolysate were partially purified by a membrane tubing below 8,000Da, the partially purified fraction remained 64.7 ${\pm}$ 3.6% of the ACE inhibition activity of the whey protein hydrolysates and IC$_{50}$ was 38.8 ${\pm}$ 2.2mg/mL. The whey-based medium was proved to be effective in producing ACE inhibitory peptides by lactic bacteria fermented whey protein.

• Korean Journal of Agricultural Science
• /
• v.39 no.4
• /
• pp.561-568
• /
• 2012

The aim of this study was to introduce a simple method for isolation of ${\alpha}$-lactalbumin, ${\beta}$-lactoglobulin and bovine serum albumin from cow's milk, and peptides produced by enzymatic hydrolysis of ${\alpha}$-lactalbumin, ${\beta}$-lactoglobulin and bovine serum albumin with alcalase. Whey protein were precipitated from whey by ammonium sulfate and, ${\alpha}$-lactalbumin and ${\beta}$-lactoglobulin were isolated using Hi Prep 26/60 Sephacryl S-100 column gel filtration chromatography. Bovine serum albumin and ${\beta}$-lactoglobulin were isolated by Mono-Q 5/50 GL column anion exchange chromatography of the 50% Ammonium Sulfate-supernatant. Isolated whey proteins were hydrolyzed by proteolytic alcalase. Tricine SDS-PAGE and reverse-phase HPLC analyses revealed that almost hydrolyzed all the ${\alpha}$-lactalbumin, ${\beta}$-lactoglobulin and bovine serum albumin with alcalase. Molecular weight of various peptides derived from alcalase hydrolysate were small molecular weight than 3.5 kDa.

• Food Science of Animal Resources
• /
• v.43 no.4
• /
• pp.594-611
• /
• 2023

Whey protein (WP) has nutritional value, but the presence of β-lactoglobulin (β-LG) and α-lactalbumin (α-LA) cause allergic reactions. In this study, hypoallergenic whey protein hydrolyate (HWPH) was prepared by decomposing β-LG and α-LA of WP using exo- and endo-type proteases. The enzyme mixing ratio and reaction conditions were optimized using response surface methodology (RSM). Degradation of α-LA and β-LG was confirmed through gel electrophoresis, and digestion, and absorption rate, and immunostimulatory response were measured using in vitro and in vivo systems. Through RSM analysis, the optimal hydrolysis conditions for degradation of α-LA and β-LG included a 1:1 mixture of Alcalase and Prozyme reacted for 10 h at a 1.0% enzyme concentration relative to substrate. The molecular weight of HWPH was <5 kDa, and leucine was the prominent free amino acid. Both in vitro and in vivo tests showed that digestibility and intestinal permeability were higher in HWPH than in WP. In BALB/c mice, as compared to WP, HWPH reduced allergic reactions by inducing elevated Type 1/Type 2 helper T cell ratio in the blood, splenocytes, and small intestine. Thus, HWPH may be utilized in a variety of low allergenicity products intended for infants, adults, and the elderly.

• Journal of Dairy Science and Biotechnology
• /
• v.26 no.1
• /
• pp.27-36
• /
• 2008

This review was written to introduce updated data on the structure and function of the major milk proteins identified as allergens, the characterization of their epitopes in each allergenic milk proteins, and the reduction of milk protein allergenicity. Most mammalian milk protein, even protein present at low concentration, are potential allergens. Epitopes identified in milk proteins are both conformational(structured epitope) and sequential epitopes(linear epitope), throughout the protein molecules. Epitopes on casein and whey proteins are reported to be sequential epitope and conformational epitopes, respectively. Conformational epitopes on whey protein are changed into sequential epitope by heat denaturation during heat treatment. Several methods have been proposed to reduce allergenicity of milk proteins. Most ideal and acceptable method to make hypoallergenic milk or formula, so far, is the hydrolysis of allergenic milk proteins by enzymes that has substrate specificity, such as pepsin, trypsin, or chymotrypsin. Commercial formulas based on milk protein hydrolysate are available for therapeutic purpose, hypoantigenic formula for infants from families with a history of milk allergy and hypoallergenic formula for infants with existing allergic symptoms.