Biological activities of the protein hydrolysate obtained from two fishes common in the fisheries bycatch

2020 ◽  
pp. 128361
Author(s):  
Tavani Rocha Camargo ◽  
Patrícia Ramos ◽  
José M. Monserrat ◽  
Carlos Prentice ◽  
Célio J.C. Fernandes ◽  
...  
2021 ◽  
Author(s):  
Rania Jacob ◽  
Hazem Hassan ◽  
Adel Afify ◽  
Gamal Gabr

Abstract Leather industries covers a wide chain of production and indirectly contributes to the economic flow. The different stages used in leather processing led to produce huge solid waste volumes. Because of the great effectiveness of amino acids as naturally chelates for minerals, the present study was carried out to recycling leather waste into its protein hydrolysate by CaO hydrolysis. The Leather protein hydrolysates (LPHs) was used to prepare metal-leather protein hydrolysate chelates (Cu2+-, Zn2+-& Fe2+-LPHCs) and some of their physical properties (i.e. λ-max, FTIR spectra, color, melting point) and biochemical properties as its antibacterial activity, as well as using as micronutrient elements for plant were evaluated. Results showed that the Cu2+-LPHC gave the highest value of melting point and λ-max than other chelates. All chelates shifted the vibration bands toward a higher frequency than LPH/CaO. Metal-leather protein hydrolysate (M-LPHCs) had antibacterial activities against E. coli, B. cereus and Micrococcus spp. mostly with Zn-LPHC and Fe-LPHC. These complexes also increased the growth characteristics and mineral absorption of spinach plants in hydroponic nutrient solution than that of mineral salts (CuSO4, ZnSO4 and FeSO4). Finally, the study concluded that M-LPHCs can be used as antimicrobial agent, micronutrients for plant and support the minerals bioavailability in animals.


Foods ◽  
2022 ◽  
Vol 11 (2) ◽  
pp. 194
Author(s):  
Xin Fan ◽  
Huimin Guo ◽  
Cong Teng ◽  
Biao Zhang ◽  
Christophe Blecker ◽  
...  

Quinoa peptides are the bioactive components obtained from quinoa protein digestion, which have been proved to possess various biological activities. However, there are few studies on the anticancer activity of quinoa peptides, and the mechanism has not been clarified. In this study, the novel quinoa peptides were obtained from quinoa protein hydrolysate and identified by liquid chromatography–tandem mass spectrometry (LC–MS/MS). The anticancer activity of these peptides was predicted by PeptideRanker and evaluated using an antiproliferative assay in colon cancer Caco-2 cells. Combined with the result of histone deacetylase 1 (HDAC1) inhibitory activity assay, the highly anticancer activity peptides FHPFPR, NWFPLPR, and HYNPYFPG were screened and further investigated. Molecular docking was used to analyze the binding site between peptides and HDAC1, and results showed that three peptides were bound in the active pocket of HDAC1. Moreover, real-time quantitative polymerase chain reaction (RT-qPCR), and Western blot showed that the expression of HDAC1, NFκB, IL-6, IL-8, Bcl-2 was significantly decreased, whereas caspase3 expression showed a remarkable evaluation. In conclusion, quinoa peptides may have the potential to protect against cancer development by inhibiting HDAC1 activity and regulating the expression of the cancer-related genes, which indicates that these peptides could be explored as functional foods to alleviate colon cancer.


2020 ◽  
Vol 74 (5) ◽  
pp. 327-339
Author(s):  
Neda Pavlovic ◽  
Jelena Jovanovic ◽  
Verica Djordjevic ◽  
Bojana Balanc ◽  
Branko Bugarski ◽  
...  

Soy proteins known for their high nutritional value and pronounced techno-functional properties, can be hydrolyzed by using proteolytic enzymes and thus converted into hydrolysates rich in di-, tri- and oligopeptides. The resulting peptides are carriers of valuable biological activities, which make the soy hydrolysates very important in functional food applications as techno-functional and bioactive ingredients. However, commercial incorporation and application of soy protein hydrolysates can be hinderedby their low bioavailability and instability, bitter taste, hygroscopicity and possibility to interact with the food matrix. The aim of this research is encapsulation of the soy protein hydrolysate in liposomes in order to overcome the stated shortcomings, while preserving the biological activities that protein hydrolysates exhibit. The soy hydrolysate was prepared by a two-step enzymatic hydrolysis of a soy protein concentrate using commercial food-grade proteases, endoprotease from Bacillus amyloliquefaciens (Neutrase?) and egzo- and endoprotease from Aspergillus oryzae (Flavourzyme?) and encapsulated within liposomes. The liposomes were produced by a thin film method using a commercial lipid mixture (Phospolipon? 90G) containing mainly phosphatidylcholine. Next, the obtained multilamellar vesicles (MLV) with the soy protein hydrolysate were treated by high-intensity ultrasound waves generated by using (1) an ultrasonic probe at a frequency of 20 kHz and (2) an ultrasonic bath with a frequency 40 kHz. The smallest (310 nm) and uniform (unimodal size distribution) liposomes with the highest efficiency of peptide encapsulation (19 %) were obtained by the probe sonication. The presented results showed that incorporation of the soy protein hydrolysates was achieved within the liposome membrane and caused an increase in the liposome size in all tested formulations, namely: from 297 to 310 nm by using the ultrasonic probe, from 722 to 850 nm by using the ultrasonic bath, while in formulations without the ultrasonic treatments the increase from 2818 to 3464 nm was recorded. The entrapped peptides caused enlargement of all liposomes and the increase in negative charge of zeta potential values, which in the case of MLV liposomes was below -30 mV, indicating high stability of these liposomes. Significant antioxidant activity of the probe-sonicated liposomal formulation was confirmed by the ABTS scavenging ability and iron-chelating activity. Release studies conducted under simulated gastrointestinal conditions confirmed that liposomes provide prolonged release of encapsulated soy protein hydrolysates as compared to diffusion of the free hydrolysate. In the first 75 min, only 20 % of liposome encapsulated soy peptides diffused, which is 2.2-fold lower as compared to the diffusion of the non-encapsulated soy hydrolysate. Liposome encapsulated soy protein hydrolysates may provide the possibility for application in the areas such as food science and technology, with the aim to enhance the nutritional value and shelf life of food products, and develop functional foods.


Foods ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 1217
Author(s):  
Seyadeh Narges Mazloomi ◽  
Leticia Mora ◽  
M-Concepción Aristoy ◽  
Alireza Sadeghi Mahoonak ◽  
Mohammad Ghorbani ◽  
...  

In this study, orange seed proteins were hydrolyzed by Alcalase enzyme at different enzyme concentrations 1–3% (v/w) and hydrolysis times (2–5 h), to obtain bioactive peptides showing antioxidant, Angiotensin-converting enzyme (ACE) -inhibitory, and hypoglycemic activities. The highest biological activities (p < 0.05) were achieved by using a hydrolysis time of 5 h and an enzyme concentration of 2%. Orange seed protein hydrolysate (OSPH) was prepared under these conditions, and peptides were isolated and purified by using size-exclusion chromatography and high-performance liquid chromatography, respectively. The fractions that showed the highest biological activities were analyzed by mass spectrometry in tandem, and a total of 63 peptide sequences were found. Moreover, the effect of simulated gastrointestinal digestion on the bioactivity of the fractions was studied, and the novel peptide sequences generated were also identified. Overall, despite there being some differences in the profile of peptide sequences obtained, the main results showed non-significant differences in the analyzed bioactivities after simulated gastrointestinal digestion.


2017 ◽  
Vol 1 (1) ◽  
pp. 24
Author(s):  
Ketut Ratnayani ◽  
Indriani Wisnu Susanto Panjaitan ◽  
Ni Made Puspawati

Abstract Protein hydrolysate contains a mixture of various lengths of short peptides chain and free amino acids that may excert biological activities. This research aims to screen potential antioxidant and antibacterial activities of protein hydrolysate produced from three kinds of germinated beans i.e. lablab bean (Lablab purpureus), pigeon pea (Cajanus cajan (L.) Millsp) and kidney bean (Phaseolus vulgaris) through enzymatic hydrolysis process. The steps of research included germination process of the beans prior to total protein isolation, enzymatic hydrolysis of total protein isolates using pancreatin enzyme, evaluation of in vitro antioxidant activity of the hydrolysates protein using DPPH (1,1-diphenyl-2-picryl hydrazyl) method, and antibaterial activity testing towards Eschericia coli and Staphyllococcus aureus bacteria. The results revealed that pancreatine enzyme was able to hydrolyse germinated protein of lablab bean, pigeon pea and kidney bean at the experiment condition applied with degree of hydrolysis 34.12%, 27.44%, and 30,93% respectively. It was also found that protein hydrolysates of lablab bean, pigeon pea, and kidney bean demonstrated antioxidant activity which percentage radical DPPH scavenging activity of 84.02%, 68.97% and 67.89 %. On the other hand, all of those protein hydrolysates did not show any antibacterial activity towards Eschericia coli and Staphyllococcus aureus bacteria.


2021 ◽  
Author(s):  
Fadoua Jabeur ◽  
Sondes Mechri ◽  
Fethi Mensi ◽  
Ines Gharbi ◽  
Yosri Ben Naser ◽  
...  

Abstract The diversity of marine biomasses is a set of exploitable and renewable resources with application in several sectors. In this context, a co-culture based on three protease-producing bacterial isolates namely; Aeribacillus pallidus VP3, Lysinibacillus fusiformis C250R, and Anoxybacillus kamchatkensis M1V strains, was carried out in a medium based on the blue swimming crab Portunus segnis bio-waste. Proteases production was optimized using a central composite design (CCD). The highest level of proteases production obtained was 8,809 U/mL in a medium comprising 75 g/L of Portunus segnis by-product powder (Pspp). The biological value of Pspp and its obtained derivates were evidenced via accredited protocols. The recovered protein hydrolysate (PHyd) was found to be active towards radical scavenging power, and against angiotensin I-converting enzyme (ACE). The blue crab chitin (BC) extraction efficiency was achieved with a yield of 32%. Afterward, chitosan was prepared through chitin N-deacetylation with a yield of 52%, leading to an acetylation degree (AD) of 19% and solubility of 90%. In addition, chitosan is found to be active against the growth of all pathogenic bacteria tested.


2017 ◽  
Vol 87 (3-4) ◽  
pp. 191-200 ◽  
Author(s):  
Nidhal Soualeh ◽  
Aliçia Stiévenard ◽  
Elie Baudelaire ◽  
Rachid Soulimani ◽  
Jaouad Bouayed

Abstract. In this study, cytoprotective and antioxidant activities of Rosa canina (RC) and Salix alba (SA), medicinal plants, were studied on mouse primary splenocytes by comparing Controlled Differential Sieving process (CDSp), which is a novel green solvent-free process, versus a conventional technique, employing hydroethanolic extraction (HEE). Thus, preventive antioxidant activity of three plant powders of homogeneous particle sizes, 50–100 µm, 100–180 µm and 180–315 µm, dissolved directly in the cellular buffer, were compared to those of hydroethanolic (HE) extract, at 2 concentrations (250 and 500 µg/mL) in H2O2-treated spleen cells. Overall, compared to HE extract, the superfine powders, i. e., fractions < 180 µm, at the lowest concentration, resulted in greater reactive oxygen species (ROS) elimination, increased glutathione peroxidase (GPx) activity and lower malondialdehyde (MDA) production. Better antioxidant and preventive effects in pre-treated cells were found with the superfine powders for SA (i. e., 50–100 µm and 100–180 µm, both p < 0.001), and with the intermediate powder for RC (i. e., 100–180 µm, p < 0.05) versus HE extract. The activity levels of catalase (CAT) and superoxide dismutase (SOD) in pretreated splenocytes exposed to H2O2, albeit reduced, were near to those in unexposed cells, suggesting that pretreatment with the fine powders has relatively restored the normal levels of antioxidant-related enzymes. These findings supported that CDSp improved the biological activities of plants, avoiding the use of organic solvents and thus it could be a good alternative to conventional extraction techniques.


2017 ◽  
Vol 12 (9) ◽  
pp. 647-651 ◽  
Author(s):  
Fatemeh Sadeghi ◽  
Abolfazl Yazdanpanah ◽  
Amirbabak Abrishamkar ◽  
Fatholah Moztarzadeh ◽  
Arash Ramedani ◽  
...  

Planta Medica ◽  
2009 ◽  
Vol 75 (09) ◽  
Author(s):  
KHC Baser ◽  
B Demirci ◽  
G Ozek ◽  
A Duran ◽  
N Tabanca ◽  
...  

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