scholarly journals Production of whey protein hydrolyzates and its incorporation into milk

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
Jenny Ann John ◽  
Bikash C. Ghosh
Keyword(s):  
Molecular Weight ◽  
Whey Protein ◽  
Whey Proteins ◽  
Ace Inhibition ◽  
Enzymatic Digestion ◽  
Whey Protein Concentrate ◽  
Low Molecular Weight ◽  
Degree Of Hydrolysis ◽  
Control Milk ◽  
Enriched Milk

Abstract Whey proteins provide an excellent source of low-molecular-weight bioactive peptides with important functional properties and bioactivities like antihypertensive, opioid, and antimicrobial effects. Presence of peptide molecules with lower molecular weight has a great role in food for health promotion. In this investigation, the release of low-molecular-weight peptides from whey protein concentrate was attempted by using enzymatic digestion. The hydrolyzate was then incorporated into milk to obtain enriched milk (EM) with low-molecular-weight peptides. Based on sensory analysis of EM, electrophoretic and RP-HPLC studies, hydrolyzates of 10% protein (degree of hydrolysis 5%; enzyme/ substrate E/S, 1:50) were finally incorporated into milk at 20% (v/v) to develop an acceptable product enriched with low-molecular-weight peptides. EM had higher protein content, viscosity and emulsifying properties than control milk with 3% fat. It is recommended that EM should not be sterilized as it results in coagulation, but can be safely pasteurized and spray dried without any undesirable effects. Maximum ACE-inhibition activity was obtained in hydrolyzate, followed by EM. This study is expected to boost the opportunity for the dairy industry to venture further into the nutraceutical dairy market. Graphical abstract

scholarly journals Enrichment of Lassi by incorporation of peptides from whey protein concentrate

2017 ◽  
Vol 9 (4) ◽  
pp. 2391-2399
Author(s):  
Preeti Paul ◽  
Bikash C. Ghosh
Keyword(s):  
Whey Protein ◽  
Whey Proteins ◽  
Age Groups ◽  
Control Sample ◽  
Whey Protein Concentrate ◽  
Degree Of Hydrolysis ◽  
Total Carbohydrate ◽  
Average Composition ◽  
Quality Product ◽  
Total Carbohydrates

Lassi is a refreshing beverage which is widely consumed throughout our country by people of all age groups. It is a reservoir of nutrients which are easily assimilable by the human body. The current study was initiated to increase functionality of Lassi by incorporation of hydrolyzed whey proteins. A solution of 10% whey protein was hydrolyzed to 7 % degree of hydrolysis (DH) using Flavorzyme at 50 0C for 30 min. using 1:25 enzyme: substrate ratio. Calculated amount of cream and lactic acid were added to the hydrolyzate to bring the desired fat content and pH levels to that of Dahi. It was found that the hydrolyzate could be incorporated at 40 % v/v level in Dahi without causing any adverse effect on the sensory attributes of Lassi. It was found that addition of sugar @15% (w/w) of Lassi gave acceptable quality product. The average composition of optimized product was - 23.04 % TS, 3.78 % protein, 2.33 % fat, 0.49 % ash and 16.5 % total carbohydrates. The average composition of control Lassi was - 22.8 % TS, 1.77 % protein, 2.10% fat, 0.49 % ash and 18.44 % total carbohydrate. The presence of low molecular weight peptides in the optimized product using Tricine SDS-PAGE was confirmed. Enriched Lassi was found to have 79.67 % ACE inhibitory activity as opposed to 42.17 % activity in control sample. It was found that non-thermized enriched Lassi sample had a shelf life of 9 days at 5+2 0C compared to 14 days for thermized sample.

Acid-labile poly(amino alcohol ortho ester) based on low molecular weight polyethyleneimine for gene delivery

2017 ◽  
Vol 32 (3) ◽  
pp. 349-361 ◽  
Author(s):  
Jun Wang ◽  
Lei Zhang ◽  
Xin Wang ◽  
Shengxiang Fu ◽  
Guoqing Yan
Keyword(s):  
Molecular Weight ◽  
Amino Alcohol ◽  
Water Solubility ◽  
Transfection Efficiency ◽  
Enzymatic Digestion ◽  
Low Molecular Weight ◽  
Hydroxyl Groups ◽  
Ortho Ester ◽  
Human Neuroblastoma ◽  
Acid Labile

A series of acid-labile poly(amino alcohol ortho ester) (POEeis) were synthesized through ring-opening polymerization between diglycidyl ethers with ortho ester bonded and low molecular weight polyethyleneimine by various feed molar ratios. The obtain POEei 1 and POEei 2 exhibited clear kinetic of degradation and condensed plasmid DNA into nanoparticles of suitable sizes (250–300 nm) and positive zeta potentials (+20–30 mV) while protecting DNA from enzymatic digestion. Further, these polymers have uniform distribution of abundant hydroxyl groups, which could improve their water solubility, biocompatibility, and lower protein adsorption. Significantly, ortho ester groups in POEeis main-chains could hydrolyze rapidly at acidic endosomal pH, resulting in intracellular DNA release and diminished material toxicity. MTT assay revealed that all the polymers exhibited much lower cytotoxicity than 25 kDa PEI in the human neuroblastoma SH-SY5Y cells. Moreover, the transfection efficiency of POEei 1 was higher than 25 kDa PEI in serum-free medium or 10% serum medium.

scholarly journals Physicochemical and sensory characteristics of whey protein hydrolysates generated at different total solids levels

2004 ◽  
Vol 72 (2) ◽  
pp. 138-143 ◽  
Author(s):  
David Spellman ◽  
Gerard O'Cuinn ◽  
Richard J FitzGerald
Keyword(s):  
Whey Protein ◽  
Whey Proteins ◽  
Reversed Phase ◽  
Protein Hydrolysates ◽  
Degree Of Hydrolysis ◽  
Total Solids ◽  
Whey Protein Hydrolysates ◽  
Peptide Peak ◽  
Hydrophobic Peptide ◽  
Physical And Chemical

Whey protein hydrolysates were generated at different total solids (TS) levels (50–300 g/l) using the commercially available proteolytic preparation Debitrase™ HYW20, while enzyme to substrate ratio, pH and temperature were maintained constant. Hydrolysis proceeded at a faster rate at lower TS reaching a degree of hydrolysis (DH) of 16·6% at 300 g TS/l, compared with a DH of 22·7% at 50 g TS/l after 6 h hydrolysis. The slower breakdown of intact whey proteins at high TS was quantified by gel-permeation HPLC. Reversed-phase (RP) HPLC of hydrolysate samples of equivalent DH (~15%) generated at different TS levels indicated that certain hydrophobic peptide peaks were present at higher levels in hydrolysates generated at low TS. Sensory evaluation showed that hydrolysates with equivalent DH values were significantly (P<0·0005) less bitter when generated at 300 g TS/l (mean bitterness score=25·4%) than hydrolysates generated at 50 g TS/l (mean bitterness score=39·9%). A specific hydrophobic peptide peak present at higher concentrations in hydrolysates generated at low TS was isolated and identified as β-lactoglobulin f(43–57), a fragment having the physical and chemical characteristics of a bitter peptide.

scholarly journals Bio-Molecular Characteristics of Whey Proteins with Relation to Inflammation

2021 ◽  
Author(s):  
Anwar Ali ◽  
Quratul Ain ◽  
Ayesha Saeed ◽  
Waseem Khalid ◽  
Munir Ahmed ◽  
...  
Keyword(s):  
Whey Protein ◽  
Protein Hydrolysate ◽  
Whey Proteins ◽  
Bovine Milk ◽  
Cost Effective ◽  
Point Of View ◽  
Whey Protein Concentrate ◽  
Molecular Characteristics ◽  
Fas Signaling ◽  
Whey Protein Hydrolysate

Whey proteins in bovine milk are a mixture of globular proteins manufactured from whey which is a byproduct of cheese industry. Whey protein is categorized to contain plethora of healthy components due to wide range of pH, promising nutritional profile with cost effective and diverse functionality. Reportedly there are three categories of whey protein, whey protein concentrate (WPC) (29–89%); whey protein isolate (WPI) 90% and whey protein hydrolysate (WPH) on the basis of proteins present in them. Whey proteins is composed of β-lactoglobulin (45–57%), immunoglobulins (10–15%) α-lactalbumin (15–25%), glicomacropeptide (10–15%), lactoperoxidase (<1%) and lactoferrin nearly (1%). Whey protein plays an important role and is validated to confer anti-inflammatory and immunostimulatory roles related to all metabolic syndromes. According to molecular point of view whey proteins decrease inflammatory cytokines (IL-1α, IL-1β, IL-10 and TNF- α); inhibits ACE and NF-κB expression; promotes Fas signaling and caspase-3 expression; elevates GLP-1, PYY, CCK, G1P and leptin; chelate and binds Fe+3, Mn+3 and Zn+2. In this chapter we will discuss significant biological role of whey proteins related to inflammatory health issues.

scholarly journals Research of changes in individual physico-chemical parameters of yoghurts using whey protein concentrates

2019 ◽  
Vol 21 (91) ◽  
pp. 162-166
Author(s):  
N. B. Slyvka ◽  
O. Ya. Bilyk ◽  
O. R. Mikhailytska ◽  
Yu. R. Hachak
Keyword(s):  
Whey Protein ◽  
Whey Proteins ◽  
Lactobacillus Delbrueckii ◽  
Whey Protein Concentrate ◽  
Protein Concentrate ◽  
Chemical Parameters ◽  
Protein Concentrates ◽  
Organoleptic Characteristics ◽  
Physico Chemical ◽  
Rate Of Decline

The purpose of the work was to investigate the effect of whey proteins and dry whey concentrates on the change of titrated and active acidity during digestion. In order to stabilize the consistency in the production of low-fat yogurts, dry whey was selected that met the requirements of State Standard 4552:2006. It is used to improve the taste of finished products, to add flavor, to improve the texture, as well as to improve overall quality. In addition, dry whey protein concentrate WPC 80 Milkiland was used. The addition of whey protein concentrate does not detract from the organoleptic characteristics of a normalized mixture, which allows it to be used in yogurt technology. The addition of whey proteins has a significant effect on the duration of gel formation. Whey protein concentrate and dry whey reduce the duration of latent fermentation and flocculation stages. The data obtained allows us to predict that they accelerate the coagulation process. This effect is enhanced by increasing the dose of protein concentrates. Conducted coagulation of milk with a different dose and observed changes in titrated and active acidity during the fermentation. Yogurt culture YF-L903, which includes Streptococcus salivarius subsp., Thermophilus, Lactobacillus delbrűeckii subsp. Bulgaricus were used for fermentation. The highest growth rate of titrated acidity is recorded for option 1 (0.5% dry sucrose) and controls that for 4 hours. the fermentation reached 80 °T. The highest rate of decline in active acidity is recorded in option 1 (0.5% dry sucrose serum). All samples for 4 hours of fermentation reached 4.65–4.72 units. pH. Thus, the acidity slightly increases with increasing the dose of serum protein concentrate and does not increase with the use of dry whey.

scholarly journals Milk Fermentation by Lacticaseibacillus rhamnosus GG and Streptococcus thermophilus SY-102: Proteolytic Profile and ACE-Inhibitory Activity

Fermentation ◽  
2021 ◽  
Vol 7 (4) ◽  
pp. 215
Author(s):  
Jessica Lizbeth Sebastián-Nicolas ◽  
Elizabeth Contreras-López ◽  
Juan Ramírez-Godínez ◽  
Alma Elizabeth Cruz-Guerrero ◽  
Gabriela Mariana Rodríguez-Serrano ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Inhibitory Activity ◽  
Ace Inhibition ◽  
Added Value ◽  
Low Molecular Weight ◽  
Ace Inhibitory Activity ◽  
Milk Fermentation ◽  
Sds Page ◽  
Ace Inhibitory

Health benefits of probiotics and production of inhibitors of angiotensin converting enzyme (ACE) released during milk fermentation are well known. That is why in this investigation the proteolytic profile and ACE inhibitory capacity of peptide fractions from protein hydrolysis of milk during fermentation processes was analyzed. Milk fermentation was carried out inoculating 106 CFU of L. rhamnosus GG, S. thermophilus SY-102 and with both bacteria. The proteolytic profile was determined using: TNBS, SDS-PAGE and SEC-HPLC techniques. In vitro ACE inhibition capacity was measured. The pH of 4.5 was reached at 56 h when the milk was fermented with L. rhamnosus, at 12 h with S. thermophillus and at 41 h in the co-culture. Production of free amino groups corresponded with the profile of low molecular weight peptides observed by SDS-PAGE and SEC-HPLC. Co-culture fermentation showed both the highest concentration of low molecular weight peptides and the ACE inhibitory activity (>80%). Results indicated that the combination of lactic cultures could be useful in manufacture of fermented milk with an added value that goes beyond basic nutrition, such as the production of ACE-inhibitory peptides.

Changes in the Distribution of Cadmium and Lead in Human and Bovine Milk Induced by Heating or Freezing

1996 ◽  
Vol 59 (1) ◽  
pp. 46-50 ◽  
Author(s):  
LUIS MATA ◽  
LOURDES SANCHEZ ◽  
PILAR PUYOL ◽  
MIGUEL CALVO
Keyword(s):  
Molecular Weight ◽  
Whey Proteins ◽  
Bovine Milk ◽  
Marked Change ◽  
Weight Fraction ◽  
Low Molecular Weight ◽  
Casein Micelles ◽  
Fat Fraction ◽  
Cadmium And Lead ◽  
Formation Of Complexes

The percentage of cadmium or lead present in the fat fraction of bovine milk is not affected by heating or freezing. In human skimmed milk, cadmium is mainly associated with a fraction with molecular weight lower than 10,000. Storage at −20°C for 10 days does not have any effect on the distribution of cadmium when milk is incubated with this metal before freezing. This treatment causes only a small increase in the amount of cadmium associated with the low molecular weight fraction when the metal is added after freezing. In bovine milk, 64% of cadmium is associated with a fraction with molecular weight above 70,000. Freezing causes a 37% decrease of the cadmium present in this fraction when the metal is added after thawing. When bovine milk was incubated with cadmium before freezing there was not a marked change in its distribution as when added after thawing. Heating at 63°C for 30 min caused a slight decrease in the amount of cadmium present in the casein fraction. The distribution change of cadmium after freezing or heating is probably due to the formation of complexes between the whey proteins and the metal, or to the disaggregation of the cadmium bound to casein micelles. Lead is mainly associated with caseins in bovine and human milk. No significant changes were caused by freezing or heating in the distribution of lead in human and bovine milk.

Acute Versus Chronic Effects of Whey Proteins on Calcium Absorption in Growing Rats

2005 ◽  
Vol 230 (8) ◽  
pp. 536-542 ◽  
Author(s):  
Yongdong Zhao ◽  
Berdine R. Martin ◽  
Meryl E. Wastney ◽  
Linda Schollum ◽  
Connie M. Weaver
Keyword(s):  
Whey Protein ◽  
Bone Mineral ◽  
Calcium Absorption ◽  
Whey Proteins ◽  
Dietary Calcium ◽  
Male Rats ◽  
Whey Protein Concentrate ◽  
Dietary Calcium Intake ◽  
Protein Concentrate ◽  
Chronic Effects

The acute and chronic effects of whey proteins on calcium metabolism and bone were evaluated. In acute studies, 8-week-old male rats were gavaged with 50 mg whey protein concentrate (WPC) and 25 mg calcium. 45Ca was administered intravenously or orally. Kinetic studies were performed, and femurs were harvested. Four of seven WPCs significantly increased femur uptake of 45Ca compared with controls. One WPC at 50 mg enhanced calcium absorption over a range of calcium Intakes from 35.1 ± 9.4% to 42.4 ± 14.0% (P < 0.01). Three of the most effective WPCs were tested further in a chronic feeding study. One hundred 3-week-old rats were randomly divided into four adequate dietary calcium (ADC; 0.4% Ca) groups (control of 20% casein and three WPC groups with 1% substitution of casein with each of three WPCs) and two low calcium (LC; 0.2% Ca) groups (control of 20% casein and one WPC group with 1% substitution of casein with one WPC). After 8 weeks, there was no effect of WPCs on femur uptake of 45Ca among ADC groups and there was no effect of WPCs on calcium retention, femur breaking force, femur bone mineral density, or total femur calcium at either dietary calcium intake. However, whole body bone mineral content (BMC) was significantly higher (P < 0.05) in the three whey protein concentrate ADC groups compared with the ADC control group. Total BMC at the proximal tibia in whey protein ADC groups was increased, as shown by peripheral quantitative computed tomography. Our results indicate that the acute calcium absorption–enhancing effect of whey proteins did not persist through long-term feeding in rats. However, the initial enhancement of calcium absorption by whey protein was sufficient to Increase BMC.

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.

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