DERIVING BIOLOGICALLY ACTIVE PEPTIDES AND STUDY Of THEIR QUALITIES

The main component of human health is nutrition which becomes even more important if a person is sick. In the body of cancer patients metabolic processes change, so he/she requires a special diet. Probiotics and short peptides are the integral part of the diet of cancer patients. One of the goals of nutritional support for cancer patients is the visceral protein pool maintenance. In modern formulae for enteral support for cancer patients the protein component can be represented in one of three types: native protein; cow’s milk whey/whole protein peptides; free amino acids. The present article deals with study on biotechnological treatment influence on milk protein controlled hydrolysis process with the aim of deriving biologically active peptides, as well as of studying several qualities: immunomodulatory, cytotoxic, antioxidant and prebiotic. Conditions for enzymic hydrolysis of milk proteins are optimised, which provide deriving biologically active directional peptides. The optimal parameters of hydrolysis conduction are chosen, which provide the polypeptide chain division into peptides and free amino acids, as well as enzymic system was chosen, consisting of chymotrypsin or thermolysin at a temperature of 37±2°C, in the enzyme-substrate ratio of 1 to 50 and process time of 12.00±0.05 h. The qualities of biologically active peptides (immunomodulatory, cytotoxic, antioxidant and prebiotic), derived from milk proteins, are studied. The studies demonstrated that all peptides under study have anti-tumour qualities, at the same time increase in biopeptide concentration causes decrease in the capacity for survival of different line cancer cells

Download Full-text

New Chemical Descriptors Relevant for the Design of Biologically Active Peptides. A Multivariate Characterization of 87 Amino Acids

Journal of Medicinal Chemistry ◽

10.1021/jm9700575 ◽

1998 ◽

Vol 41 (14) ◽

pp. 2481-2491 ◽

Cited By ~ 360

Author(s):

Maria Sandberg ◽

Lennart Eriksson ◽

Jörgen Jonsson ◽

Michael Sjöström ◽

Svante Wold

Keyword(s):

Amino Acids ◽

Biologically Active ◽

Active Peptides ◽

Biologically Active Peptides ◽

Chemical Descriptors

Download Full-text

Free Amino-acids in Human Sweat from Different Parts of the Body

Nature ◽

10.1038/215416a0 ◽

1967 ◽

Vol 215 (5099) ◽

pp. 416-417 ◽

Cited By ~ 37

Author(s):

B. HADORN ◽

F. HANIMANN ◽

P. ANDERS ◽

H.-CH. CURTIUS ◽

R. HALVERSON

Keyword(s):

Amino Acids ◽

Free Amino Acids ◽

Free Amino ◽

The Body ◽

Human Sweat ◽

Different Parts

Download Full-text

Application of Asian pumpkin (Cucurbita ficifolia) serine proteinase for production of biologically active peptides from casein.

Acta Biochimica Polonica ◽

10.18388/abp.2013_1960 ◽

2013 ◽

Vol 60 (1) ◽

Cited By ~ 6

Author(s):

Anna Dąbrowska ◽

Marek Szołtysik ◽

Konrad Babij ◽

Marta Pokora ◽

Aleksandra Zambrowicz ◽

...

Keyword(s):

Antimicrobial Activity ◽

Free Amino ◽

Serine Proteinase ◽

Biologically Active ◽

Amino Group ◽

Active Peptides ◽

Rp Hplc ◽

Amino Group Content ◽

Biologically Active Peptides ◽

Peptide Profiles

The main objective of this study was to determine potential application of a serine proteinase derived from Asian pumpkin for obtaining biologically active peptides from casein. The course of casein hydrolysis by three doses of the enzyme (50, 150, 300 U/mg of protein) was monitored for 24 hours by the determinations of: hydrolysis degree DH (%), free amino group content (μmole Gly/g), RP HPLC peptide profiles and by polyacrylamide gel electrophoresis. In all hydrolyzates analyzed antioxidant activities were determined using three tests: the ability to reduce iron ions in FRAP test, the ability to scavenge free radicals in DPPH test, and Fe(2+) chelating activity. The antimicrobial activity of obtained peptide fractions was determined as the ability to inhibit the growth of Escherichia coli, Bacillus cereus and Pseudomonas fluorescens in a diffusion plate test. The deepest degradation, expressed as the DH [%] and the free amino group content (67% and 7528 µmole Gly/mg, respectively), was noted in samples hydrolyzed with 300 U/ml of enzyme for 24 hours, while in other samples the determined values were about three and two times lower. The results were in agreement with the peptide profiles obtained by RP HPLC. The highest antioxidative activities determined in all tests were seen for the casein hydrolysate obtained with 300 U/mg protein of serine proteinase after 24 h of reaction (2.15 µM Trolox/mg, 96.15 µg Fe(3+)/mg, 814.97 µg Fe(2+)/mg). Antimicrobial activity was presented in three preparations. In other samples no antimicrobial activity was detected.

Download Full-text

Potential Anticarcinogenic Peptides from Bovine Milk

Journal of Amino Acids ◽

10.1155/2013/939804 ◽

2013 ◽

Vol 2013 ◽

pp. 1-7 ◽

Cited By ~ 29

Author(s):

Giacomo Pepe ◽

Gian Carlo Tenore ◽

Raffaella Mastrocinque ◽

Paola Stusio ◽

Pietro Campiglia

Keyword(s):

Antioxidant Activities ◽

Whey Proteins ◽

Bovine Milk ◽

The Body ◽

Biologically Active ◽

Food Science ◽

Bovine Lactoferrin ◽

Active Peptides ◽

Enzymatic Proteolysis ◽

Biologically Active Peptides

Bovine milk possesses a protein system constituted by two major families of proteins: caseins (insoluble) and whey proteins (soluble). Caseins (αS1, αS2, β, and κ) are the predominant phosphoproteins in the milk of ruminants, accounting for about 80% of total protein, while the whey proteins, representing approximately 20% of milk protein fraction, include β-lactoglobulin, α-lactalbumin, immunoglobulins, bovine serum albumin, bovine lactoferrin, and lactoperoxidase, together with other minor components. Different bioactivities have been associated with these proteins. In many cases, caseins and whey proteins act as precursors of bioactive peptides that are released, in the body, by enzymatic proteolysis during gastrointestinal digestion or during food processing. The biologically active peptides are of particular interest in food science and nutrition because they have been shown to play physiological roles, including opioid-like features, as well as immunomodulant, antihypertensive, antimicrobial, antiviral, and antioxidant activities. In recent years, research has focused its attention on the ability of these molecules to provide a prevention against the development of cancer. This paper presents an overview of antitumor activity of caseins and whey proteins and derived peptides.

Download Full-text

Water Relations in an Insect, Thermobia Domestica

Journal of Experimental Biology ◽

10.1242/jeb.58.2.385 ◽

1973 ◽

Vol 58 (2) ◽

pp. 385-400

Author(s):

A. Y. K. OKASHA

Keyword(s):

Amino Acids ◽

Water Relations ◽

Free Amino Acids ◽

Free Amino ◽

The Body ◽

Thermobia Domestica ◽

Moulting Cycle

1. The concentrations of Na+ and K+ in the haemolymph remain relatively constant during the moulting cycle. 2. Desiccation, desiccation followed by rehydration and starvation exert little or no effect on the concentrations of Na+ and K+ in the haemolymph. 3. The volume of haemolymph decreases during desiccation and increases after rehydration. 4. More Na+ is voided in the excreta during desiccation. 5. Repeated desiccation and rehydration causes the loss of both Na+ and K+ from the body. 6. The effects of desiccation and rehydration on the concentrations of chlorides and free amino acids in the haemolymph are described.

Download Full-text

Biologically active peptides of casein and lactotransferrin implicated in platelet function

Journal of Dairy Research ◽

10.1017/s002202990002879x ◽

1989 ◽

Vol 56 (3) ◽

pp. 351-355 ◽

Cited By ~ 29

Author(s):

Anne-Marie Fiat ◽

Sylviane Levy-Toledano ◽

Jacques P. Caen ◽

Pierre Jollès

Keyword(s):

Platelet Function ◽

Blood Clotting ◽

Milk Proteins ◽

Biologically Active ◽

Active Peptides ◽

Biologically Active Peptides

SummaryCasein and other milk proteins in maternal colostrum and milk, the earliest food of the newborn, should not only be considered as a nutritional supply but also as a source of biologically active peptides. Some of them isolated from casein and lactotransferrin were active on platelet function. They inhibited both aggregation of ADP-treated platelets and binding of [125I] fibrinogen to ADP-treated platelets. Their behaviour was compared to that of fibrinogen peptides possessing similar effects: once more similarities between the milk and blood-clotting phenomena could be observed.

Download Full-text

Salivary Factors that Maintain the Normal Oral Commensal Microflora

Journal of Dental Research ◽

10.1177/0022034520915486 ◽

2020 ◽

Vol 99 (6) ◽

pp. 644-649 ◽

Cited By ~ 2

Author(s):

G.H. Carpenter

Keyword(s):

Amino Acids ◽

Protein Degradation ◽

Salivary Glands ◽

Free Amino Acids ◽

Free Amino ◽

Salivary Protein ◽

The Body ◽

Oral Microbiome ◽

Normal Flora ◽

Normal Microflora

The oral microbiome is one of the most stable ecosystems in the body and yet the reasons for this are still unclear. As well as being stable, it is also highly diverse which can be ascribed to the variety of niches available in the mouth. Previous studies have focused on the microflora in disease—either caries or periodontitis—and only recently have they considered factors that maintain the normal microflora. This has led to the perception that the microflora proliferate in nutrient-rich periods during oral processing of foods and drinks and starves in between times. In this review, evidence is presented which shows that the normal flora are maintained on a diet of salivary factors including urea, lactate, and salivary protein degradation. These factors are actively secreted by salivary glands which suggests these factors are important in maintaining normal commensals in the mouth. In addition, the immobilization of SIgA in the mucosal pellicle indicates a mechanism to retain certain bacteria that does not rely on the bacterial-centric mechanisms such as adhesins. By examining the salivary metabolome, it is clear that protein degradation is a key nutrient and the availability of free amino acids increases resistance to environmental stresses.

Download Full-text