Extensive enzymatic hydrolysates of whey and colostrum proteins for specialized food

2021 ◽  
pp. 24-25
Author(s):  
Татьяна Николаевна Головач ◽  
Владимир Петрович Курченко ◽  
Владимир Александрович Асафов ◽  
Евгения Леонидовна Искакова ◽  
Нина Леонидовна Танькова
Keyword(s):  
Comparative Study ◽  
Whey Proteins ◽  
Antibacterial Effects ◽  
Peptide Profile ◽  
Enzymatic Hydrolysates

Проведено комплексное сравнительное исследование пептидного состава и биологических активностей глубоких ферментативных гидролизатов коровьего молока. Образцы гидролизованных сывороточных белков и молозива обладают подтвержденным антиоксидантным, антимутагенным и антибактериальным действием. A comprehensive comparative study of peptide profile and bioactivities of extensive enzymatic dairy hydrolysates was carried out. Samples of hydrolysed whey proteins and colostrum possess proven antioxidant, antimutagenic and antibacterial effects.

scholarly journals Production of ACE Inhibitory Peptides from Whey Proteins Modified by High Intensity Ultrasound Using Bromelain

Foods ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 2099
Author(s):  
Lucía Abadía-García ◽  
Eduardo Castaño-Tostado ◽  
Anaberta Cardador-Martínez ◽  
Sandra Teresita Martín-del-Campo ◽  
Silvia L. Amaya-Llano
Keyword(s):  
Protein Structure ◽  
Enzymatic Hydrolysis ◽  
Whey Protein ◽  
High Intensity ◽  
Whey Proteins ◽  
High Intensity Ultrasound ◽  
Peptide Profile ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

High Intensity Ultrasound (HIUS) can induce modification of the protein structure. The combination of enzymatic hydrolysis and ultrasound is an interesting strategy to improve the release of the Angiotensin-Converting Enzyme (ACE) inhibitory peptides. In this study, whey proteins were pretreated with HIUS at two levels of amplitude (30 and 50%) for 10 min, followed by hydrolysis using the vegetable protease bromelain. The hydrolysates obtained were ultrafiltrated and their fractions were submitted to a simulated gastrointestinal digestion. The conformational changes induced by HIUS on whey proteins were analyzed using Fourier-transform infrared spectroscopy by attenuated total reflectance (FTIR-ATR) and intrinsic spectroscopy. It was found that both levels of ultrasound pretreatment significantly decreased the IC50 value (50% Inhibitory Concentration) of the hydrolysates in comparison with the control (α = 0.05). After this treatment, HIUS-treated fractions were shown as smaller in size and fractions between 1 and 3 kDa displayed the highest ACE inhibition activity. HIUS promoted significant changes in whey protein structure, inducing, unfolding, and aggregation, decreasing the content of α-helix, and increasing β-sheets structures. These findings prove that ultrasound treatment before enzymatic hydrolysis is an innovative and useful strategy that modifies the peptide profile of whey protein hydrolysates and enhances the production of ACE inhibitory peptides.

scholarly journals THE EFFECT OF CAMEL MILK WHEY PROTEINS ON LACTIC ACID BACTERIA ISOLATED FROM CAMEL AND COW MILKS IN EGYPT: A COMPARATIVE STUDY.

2018 ◽  
Vol 6 (2) ◽  
pp. 986-998
Author(s):  
Mariam Mohammed ◽  
◽  
MarwaHEl Gendy ◽  
AidaS Salem ◽  
WafaiZA Mikhail ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactic Acid Bacteria ◽  
Comparative Study ◽  
Whey Proteins ◽  
Camel Milk ◽  
Milk Whey

scholarly journals IMPROVEMENT OF THE METHOD OF COMPARATIVE STUDY OF MILK WHEY PROTEINS ENZYMATIC HYDROLYSIS

2019 ◽  
Vol 5 ◽  
pp. 52-57
Author(s):  
Volodymyr Yukalo ◽  
Kateryna Datsyshyn ◽  
Liudmyla Storozh
Keyword(s):  
Enzymatic Hydrolysis ◽  
Comparative Study ◽  
Proteolytic Activity ◽  
Isoelectric Point ◽  
Whey Proteins ◽  
Gel Filtration ◽  
Biologically Active ◽  
Neutral Protease ◽  
Enzyme Preparations ◽  
Milk Whey

Milk whey proteins are valueble nutritional ingredients with a number of health-beneficial properties. Whey proteins are also a source of bioactive peptides that can be released in the process of proteins enzymatic hydrolysis. In this connection, there often is a need to compare their proteolytic action on milk whey proteins. It is important to take into account the specificities of the composition and properties of milk whey proteins. The aim of the research was to improve the method of comparative study of milk whey proteins enzymatic hydrolysis. Casein and whey were obtained from fresh cow skimmed milk. The whey was separated by centrifugation after casein precipitation at the isoelectric point. The following enzyme preparations were used in the research: neutral protease, papain, trypsin, chymotrypsin and pancreatin. To select β-LG, gel filtration of the milk whey on the chromatographic column with Sephadex G-150 (Pharmacia) was used. The homogeneity of the received β-LG preparation was analyzed by express electrophoresis in the polyacrylamide gel plates (PAG). The preparation of general casein was isolated by repeated precipitation at the isoelectric point. The fractional composition of the casein substrate was analyzed by electrophoresis in the anode system of homogeneous PAG in the presence of urea. Quantitative treatment of electrophoregrams of the β-LG preparation was performed using the imread reading function. Determination of proteolytic activity of enzyme preparations was carried out according to the method of V. F. Selemenev [6]. In the course of the research, it was determined, that for the research of proteolysis under conditions of identical total proteolytic activity, the concentration of neutral protease should be increased by 1.02 times, papain – by 4.2 times, trypsin – by 2.8 times, pancreatin – by 2.12 times as compared to chymotrypsin. As a result, it has been shown that the use of β-lactoglobulininstead of serum albumin in spectrophotometric determinations allows obtaining more accurate values of the concentrations of whey protein and proteolytic products. In determining the ratio of enzyme : substrate it is advisable to take into account the general proteolytic activity of various enzyme preparations in comparative studies of whey proteins proteolysis with various enzyme preparations. These will simplify the methodology and reduce the time for objective evaluation of enzymatic preparations for proteolysis of milk whey proteins. In some cases, considering the specificity of proteases it could increase the yield of biologically active peptides.

Degree of hydrolysis and peptide profile of whey proteins using pancreatin

Nutrire ◽  
2013 ◽  
Vol 38 (3) ◽  
pp. 278-290 ◽  
Author(s):  
Marialice Pinto Coelho Silvestre ◽  
Harriman Aley Morais ◽  
Viviane Dias Medeiros Silva ◽  
Mauro Ramalho Silva
Keyword(s):  
Whey Proteins ◽  
Degree Of Hydrolysis ◽  
Peptide Profile

scholarly journals Comparative Study on Heat Stability and Functionality of Camel and Bovine Milk Whey Proteins

2008 ◽  
Vol 91 (12) ◽  
pp. 4527-4534 ◽  
Author(s):  
L.C. Laleye ◽  
B. Jobe ◽  
A.A.H. Wasesa
Keyword(s):  
Comparative Study ◽  
Whey Proteins ◽  
Bovine Milk ◽  
Heat Stability ◽  
Milk Whey

scholarly journals COMPARATIVE STUDY OF MILK WHEY PROTEINS AND PURE CYSTINE, BY MEANS OF POLAROGRAPHY

1972 ◽  
Vol 23 (2) ◽  
pp. 104
Author(s):  
Ι. Χ. ΑΣΙΚΗΣ
Keyword(s):  
Comparative Study ◽  
Whey Proteins ◽  
Milk Proteins ◽  
Good Deal ◽  
Milk Whey ◽  
Milk Samples ◽  
Probable Consequence ◽  
Partial Destruction

In the present research, it is studied the proteins, albumin and globulin, concentration in the milk whey of three mammals, cow, goat and sheep, by means of the Polarographie method and existing similarities in comparison with pure cystine are pointed out. For 150 examined milk samples, it was followed the same technique of study, selected after a good deal of preliminary tests. Also, it is studied the height, up to which Polarographie wave it is risen, after heating the milk of the above mentioned animals from 72° to 100° C. It is proved that the decrease of Polarographie protein weaves height goes nearly parallel with the increase of temperature, that is related directly with the degree of denaturation of milk albumin and globulin, having as a very probable consequence, at least, the partial destruction of the SH/SS groups contained in milk proteins.

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