scholarly journals Synthesis, extraction and idetification of meat bioactive peptides: a review

2021 ◽  
Vol 888 (1) ◽  
pp. 012058
Author(s):  
Edy Susanto ◽  
Anik Fadlilah ◽  
Muhammad Fathul Amin

Abstract The consumption of meat should consider the concept of functional food. The meat had a highquality protein and contain of bioactive peptide compounds. Amino acid was component of bioactive peptides compound. It joined by covalent bonds known as amide or peptide bonds. A lot of research was currently focused on the bioactive peptide compounds isolated from myofibril and sarcoplasmic proteins with the synthesis, extraction, and identification methods. This study used a systematic review to get the structure of amino acids that the source of bioactive components and the principle of synthesis, extraction and identification of bioactive peptide in the meat. This paper highlights were finding on the structure of amino acid in the meat. The proportion of amino acids was also different in each animal body location. The result identified that more than 170 peptides were released from the main structure of the myofibril (actin, myosin) and sarcoplasmic muscle proteins, and the synthesis, extraction and bioactive peptide identification in the meat as well as their potential use as functional food.

2021 ◽  
Author(s):  
Irina Gaivoronskaya ◽  
Valenitna Kolpakova

The aim of the work was to optimize the process of obtaining multicomponent protein compositions with high biological value and higher functional properties than the original vegetable protein products. Was realized studies to obtain biocomposites on the base of pea protein-oat protein and pea protein-rice protein. Developed composites were enriched with all limited amino acids. For each of the essential amino acids, the amino acid score was 100% and higher. Protein products used in these compositions are not in major allergen list, which allows to use these compositions in allergen-free products and specialized nutrition. To determine biosynthesis parameters for compositions from pea protein and various protein concentrates with the use of transglutaminase enzyme, was studied effect of concentration and exposition time on the amount of amino nitrogen released during the reaction. Decreasing of amino nitrogen in the medium indicated the occurrence of a protein synthesis reaction with the formation of new covalent bonds. Were determined optimal parameters of reaction: the hydromodule, the exposure time, the concentration of EP of the preparation, were obtained mathematical models. Studies on the functional properties of composites, the physicochemical properties of the proteins that make up their composition, and structural features will make it possible to determine the uses in the manufacture of food products based on their ability to bind fat, water, form foam, gels, and etc.


2019 ◽  
Vol 20 (23) ◽  
pp. 5978 ◽  
Author(s):  
Minkiewicz ◽  
Iwaniak ◽  
Darewicz

The BIOPEP-UWM™ database of bioactive peptides (formerly BIOPEP) has recently become a popular tool in the research on bioactive peptides, especially on these derived from foods and being constituents of diets that prevent development of chronic diseases. The database is continuously updated and modified. The addition of new peptides and the introduction of new information about the existing ones (e.g., chemical codes and references to other databases) is in progress. New opportunities include the possibility of annotating peptides containing D-enantiomers of amino acids, batch processing option, converting amino acid sequences into SMILES code, new quantitative parameters characterizing the presence of bioactive fragments in protein sequences, and finding proteinases that release particular peptides.


1983 ◽  
Vol 3 (1_suppl) ◽  
pp. 10-12 ◽  
Author(s):  
Oimitrios G. Oreopoulos ◽  
Errol Marliss G. Harvey ◽  
Anderson Arie Oren ◽  
Nicholas Oombros Paul ◽  
Williams Ramesh Khanna ◽  
...  

As a result of a combination of a decreased appetite with increased nutrient losses in the dialysate, a number of CAPO patients may develop malnutrition. A decrease in appetite is also observed in normal animals undergoing CAPO which suggests that some factors related to CAPO influence appetite so that these animals eat less. In addition to protein losses, CAPO patients are losing approximately two grams of amino acids a day, and they have plasma amino acid abnormalities similar to those produced by malnutrition and uremia. An amino acid-containing dialysis solution (2%) is an effective solution with respect to ultrafiltration and solute removal. Amino acids can be absorbed by the peritoneal route and produce an increase in plasma amino acids to levels similar to those observed after a protein meal. These observations indicate that administration of amino acids via the peritoneal route may prevent or correct malnutrition developed in patients on CAPO.


Soil Research ◽  
1966 ◽  
Vol 4 (1) ◽  
pp. 41 ◽  
Author(s):  
JN Ladd ◽  
JHA Butler

Twenty-three model phenolic polymers, either nitrogen-free or incorporating amino acids, peptides, or proteins, have been prepared from p-benzoquinone and catechol under mild oxidative conditions. Two lines of experimentation have demonstrated properties of soil humic acids closely similar to those of polymers incorporating proteins, but different from those of polymers incorporating amino acids: (1) fractionation of humic acids and synthetic polymers by 'Sephadex' gel filtration showed that the percentage of components of molecular weights nominally greater than 100 000 ranged from 52-76 % for eight humic acids tested, 53-59 % for benzoquinone-protein polymers (excluding polymers containing protamine), but less than 20% for all other polymers; (2) acid hydrolysis with 6M HCl resulted in a partial release of polymer nitrogen. Amino acid nitrogen in the hydrolysates accounted for 32.4-51.9 % of humic acid nitrogen, 31.2-56.3 % of the nitrogen of polymers incorporating protein, but less than 10.8% of the nitrogen of polymers incorporating individual amino acids. Experiments with model monomeric N-phenylglycine derivatives and with polymers incorporating simple peptides showed that the bond between the carbon atom of an aromatic ring and the nitrogen atom of an a-amino acid is far more stable to acid hydrolysis than peptide bonds or bonds linking amino acids in humic acids. Glycine is, however, readily released from N-phenylglycine derivatives when conditions favour their oxidation to a quinone-imine intermediate. Incorporation of proteins into phenolic polymers prevented the detection of peptide bonds by the Folin reagent.


2021 ◽  
Vol 27 ◽  
Author(s):  
Maria Hayes

: Food derived bioactive peptides can be generated from various protein sources and usually consist of between 2-30 amino acids with bulky, side-chain aromatic amino acids preferred in the ultimate and penultimate positions at the Cterminal end of the amino acid chain. They are reported to impart a myriad of preventative health beneficial effects to the consumer once ingested and these include heart health benefits through inhibition of enzymes including renin (EC 3.4.23.15) and angiotensin-I-converting enzyme (ACE-I; EC 3.4.15.1) within the renin angiotensin aldosterone system (RAAS); anti-inflammatory (due to inhibition of ACE-I and other enzymes) and anti-cancer benefits; prevention of type-2 diabetes through inhibition of dipeptidyl peptidase IV (DPP-IV), bone and dental strength, antimicrobial and immunomodulatory effects and several others. Peptides have also reported health benefits in the treatment of asthma, neuropathic pain, HIV and wound healing. However, the structure, amino acid composition and length of these peptides along with the quantity of peptide that can pass through the gastrointestinal tract and often the blood brain barrier (BBB) intact and reach the target organ is important for the realisation of these health effects in an in vivo setting. This paper aims to collate recent important research concerning the generation and detection of peptides in the laboratory. It discusses products currently available as preventative healthcare peptide options and relevant legislation barriers to place a food peptide product on the market. The review also highlights useful in silico computer based methods and analysis that may be used to generate specific peptide sequences from proteins whose amino acid sequences are known and also to determine if the peptides generated are unique and bioactive. The topic of food-derived bioactive peptides for health is of great interest to scientific research and industry due to evolving drivers in food product innovation including health and wellness for the elderly, infant nutrition and optimum nutrition for sports athletes as well as the humanisation of pets. This paper provides an overview of what is required to generate bioactive peptide containing hydrolysates; what methods should be used in order to characterise the health beneficial effects of these hydrolysates and the active peptide sequences, potential applications of bioactive peptides and legislative requirements in Europe and the United States. It also highlights success stories and barriers to the development of peptide containing food products that currently exist.


Food Research ◽  
2020 ◽  
Vol 4 (5) ◽  
pp. 1663-1669
Author(s):  
K. Hinokidani ◽  
S. Koyama ◽  
M. Irie ◽  
Y. Nakanishi

Herbal remedies by using mangrove plants have been recognized in several countries, and the plant materials are often consumed as a tea, which are infusions of dried plant parts steeped in boiling water. These infusions from mangrove plants are believed to be effective agents for treating and/or prevent infections, ailments, and diseases, and some mangrove plants have attracted attention as functional food resources in recent years. To reveal the beneficial properties of mangrove plants, clarification of the chemical ingredient and its characteristics of mangrove plants is required. This study focused on amino acids, which were functional ingredients (i.e., bioactive compounds) because amino acids are expected to function as ‘functional ingredients’ in addition to conventional ‘nutrients’ in recent years. To demonstrate the further possibilities of mangrove tea, we firstly evaluated the content of total amino acids in the leaf of several dominant mangrove species with commercial teas as references. Next, we clarified the composition of amino acids by using LC-MS analysis. As the results, free amino acid content (FAC) in leaf sample of Rhizophora stylosa, Bruguira gymnorrhiza, Kandelia obovata, Avicennia marina, Sonneratia alba, and Lumnitzera racemosa was 747, 1056, 946, 829, 623, and 896 mg/100 g DW, respectively. The FAC in all mangrove leaf samples were higher than those in green tea of low price, black tea, oolong tea, barley tea, and mate tea. Moreover, it was found that GABA accounts for over 10% of the total amino acid in the mangrove leaf samples. Especially in mature leaves of K. obovata, the ratio was very high levels 35%. In the case of K. obovata, the contents were higher than GABA tea. Based on this, we concluded that several mangrove plants, especially K. obovata has the potential of a functional food which is GABA-rich.


2021 ◽  
Vol 9 (2) ◽  
pp. 118-123
Author(s):  
Healthy Kainama ◽  
Hanoch J. Sohilait ◽  
Christian Jacob Souisa

Gastropods are the sources of protein for coastal communities in the Maluku islands. We conducted analysis quantitative and qualitative of protein in Nerita undata meat from Hasa Cape in Saparua Island. The percentage of protein was analyzed by the Kjeldahl method. Qualitative analysis began with breaking peptide bonds in protein to amino acid components by sulphuric acid and barium hydroxide hydrolyzed. We identified amino acid compounds by using thin-layer chromatography (TLC) in butanol-acetic acid-water (8:1:1, v/v) as eluent. The result showed that N. undata meat contains 11.15% of protein and twelve amino acid compounds. There are seven essential amino acids in N. undata meat from supralittoral rocks and mezolittoral zone of Hasa cape is a source of quality protein. Thus, this species can be considered as a source of high-quality protein.


2008 ◽  
Vol 91 (4) ◽  
pp. 894-900 ◽  
Author(s):  
G Sarwar Gilani ◽  
Chaowu Xiao ◽  
Nora Lee

Abstract Accurate standardized methods for the determination of amino acid in foods are required to assess the nutritional safety and compositional adequacy of sole source foods such as infant formulas and enteral nutritionals, and protein and amino acid supplements and their hydrolysates, and to assess protein claims of foods. Protein digestibility-corrected amino acid score (PDCAAS), which requires information on amino acid composition, is the official method for assessing protein claims of foods and supplements sold in the United States. PDCAAS has also been adopted internationally as the most suitable method for routine evaluation of protein quality of foods by the Food and Agriculture Organization/World Health Organization. Standardized methods for analysis of amino acids by ion-exchange chromatography have been developed. However, there is a need to develop validated methods of amino acid analysis in foods using liquid chromatographic techniques, which have replaced ion-exchange methods for quantifying amino acids in most laboratories. Bioactive peptides from animal and plant proteins have been found to potentially impact human health. A wide range of physiological effects, including blood pressure-lowering effects, cholesterol-lowering ability, antithrombotic effects, enhancement of mineral absorption, and immunomodulatory effects have been described for bioactive peptides. There is considerable commercial interest in developing functional foods containing bioactive peptides. There is also a need to develop accurate standardized methods for the characterization (amino acid sequencing) and quantification of bioactive peptides and to carry out dose-response studies in animal models and clinical trials to assess safety, potential allergenicity, potential intolerance, and efficacy of bioactive peptides. Information from these studies is needed for determining the upper safe levels of bioactive peptides and as the basis for developing potential health claims for bioactive peptides. This information is, in turn, needed by regulatory agencies for developing appropriate policy and regulations on adding these substances to foods and for determining if health claims are scientifically substantiated.


1997 ◽  
Vol 324 (2) ◽  
pp. 517-522 ◽  
Author(s):  
Antonio. C. M CAMARGO ◽  
Marcelo. D GOMES ◽  
Antonia. P REICHL ◽  
Emer. S FERRO ◽  
Saul JACCHIERI ◽  
...  

A systematic analysis of the peptide sequences and lengths of several homologues of bioactive peptides and of a number of quenched-fluorescence (qf) opioid- and bradykinin-related peptides was performed to determine the main features leading the oligopeptides to hydrolysis by the recombinant rat testis thimet oligopeptidase (EC 3.4.24.15). The results indicate that a minimum substrate length of six amino acids is required and that among the oligopeptides six to thirteen amino acid residues long, their susceptibility as substrates is highly variable. Thimet oligopeptidase was able to hydrolyse, with similar catalytic efficiency, peptide bonds having hydrophobic or hydrophilic amino acids as well as proline in the P1 position of peptides, ranging from a minimum of six to a maximum of approximately thirteen amino acid residues. An intriguing observation was the shift of the cleavage site, at a Leu-Arg bond in qf dynorphin-(2–8) [qf-Dyn2–8; Abz-GGFLRRV-EDDnp, where Abz stands for o-aminobenzoyl and EDDnp for N-(2,4-dinitrophenyl) ethylenediamine], to Arg-Arg in qf-Dyn2–8Q, in which Gln was substituted for Val at its C-terminus. Similarly, a cleavage site displacement was also observed with the hydrolysis of the internally quenched-fluorescence bradykinin analogues containing Gln at the C-terminal position, namely Abz-RPPGFSPFR-EDDnp and Abz-GFSPFR-EDDnp are cleaved at the Phe-Ser bond, but Abz-RPPGFSPFRQ-EDDnp and Abz-GFSPFRQ-EDDnp are cleaved at the Pro-Phe bond.


2012 ◽  
Vol 2 (10) ◽  
pp. 325 ◽  
Author(s):  
Nora Khaldi

The traditional methods for mining foods for bioactive peptides are tedious and long. Similar to the drug industry, the length of time to identify and deliver a commercial health ingredient that reduces disease symptoms can take anything between 5 to 10 years. Reducing this time and effort is crucial in order to create new commercially viable products with clear and important health benefits. In the past few years, bioinformatics, the science that brings together fast computational biology, and efficient genome mining, is appearing as the long awaited solution to this problem. By quickly mining food genomes for characteristics of certain food therapeutic ingredients, researchers can potentially find new ones in a matter of a few weeks. Yet, surprisingly, very little success has been achieved so far using bioinformatics in mining for food bioactives. The absence of food specific bioinformatic mining tools, the slow integration of both experimental mining and bioinformatics, and the important difference between different experimental platforms are some of the reasons for the slow progress of bioinformatics in the field of functional food and more specifically in bioactive peptide discovery. In this paper I discuss some methods that could be easily translated, using a rational peptide bioinformatics design, to food bioactive peptide mining. I highlight the need for an integrated food peptide database. I also discuss how to better integrate experimental work with bioinformatics in order to improve the mining of food for bioactive peptides, therefore achieving a higher success rates.Keywords: bioactive peptides, bioinformatics, mining food, therapeutic properties, food proteins, functional food.


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