Influence of Selected Packaging Materials on Quality Aspects of High Pressure Processed Boccoli Puree

In the present study, role of packaging properties on pressure and thermal processed broccoli puree quality were investigated. Samples were packaged in two multilayer packaging pouches (PET/PA/LLLDPE and BOPP/LLDPE). Packaging type significantly influenced the product colour. PET/PA/LLLDPE package best preserved broccoli puree quality. Thermal processes at both intensity levels, had a significant effect on quality properties of broccoli puree. Tensile strength of both packaging materials were improved by severe HP and thermal pasteurization. The shape of endothermic heating curves of both packaging materials as well as Tg value of BOPP/LLDPE, compromised by conventional thermal treatments. High pressure processing at 600 MPa (holding time: 10 min/initial temperature: 10 °C) improved the colour (a* and L* values) compared to severe HP pasteurization and thermal pasteurization processes. Both packaging materials resulted in inactivation of the inoculated Listeria innocua to a level below the detection limit at HP and thermally processed broccoli pure. Keywords: Packaging material, Broccoli, Puree, Thermal processing, High pressure processing, Barrier propertie

Royal Jelly: Chemistry, Storage and Bioactivities

Royal jelly (RJ) has been known for centuries, but in the last 5-6 decades its systematic production and consumption has increased. RJ is secreted by the hypopharyngeal and mandibular glands of worker honeybees (Apis mellifera). This thick and milky substance contains water, proteins, carbohydrates, lipids, minerals, vitamins and such bio-active compounds as acetylcholine, peptides, the hormones testosterone, progesterone, prolactin, estradiol, (hydroxydecanoic acid) (HAD), adenosine monophosphate (AMP)-N1Oxide, polyphenols, flavonoids and adenosine. Because of its bioactive compounds, RJ can be considered as a functional and nutraceutical food. The main goal of this review is to summarize and update its physicochemical properties, bio-active ingredients, storage stability and shelf life. The functional properties are antioxidative activity, insulin-like action, improvement against diabetes, liver protection, antitumoral action, neurotrophic action, antibiotic effect, anti-inflammatory action and wound healing, hypotensive effect and blood regulatory actions, anti-aging effect and skin protection, effects on the reproductive system and fertility and also fortifying, tonic action and immunomodulating and anti-alergic activity. RJ may cause allergic reactions, asthma and even fatal anaphylaxis in some humans. Therefore, RJ should be orally ingested as nutreaceutical agent or food-ingredient only after an allergy test

Royal jelly: Chemistry, storage and bioactivities

Royal jelly (RJ) has been known for centuries, but in the last 5-6 decades its systematic production and consumption has increased. RJ is secreted by the hypopharyngeal and mandibular glands of worker honeybees (Apis mellifera). This thick and milky substance contains water, proteins, carbohydrates, lipids, minerals, vitamins and such bio-active compounds as acetylcholine, peptides, the hormones testosterone, progesterone, prolac-tin, estradiol, (hydroxydecanoic acid) (HAD), adenosine monophosphate (AMP)-N1Oxide, polyphenols, flavonoids and adenosine. Because of its bioactive compounds, RJ can be considered as a functional and nutraceutical food. The main goal of this review is to summarize and update its physicochemical properties, bio-active ingredients, storage stability and shelf life. The functional properties are antioxidative activity, insulin-like action, improvement against diabetes, liver protection, antitumoral action, neurotrophic action, antibiotic effect, anti-inflammatory action and wound healing, hypotensive effect and blood regulatory actions, anti-aging effect and skin protection, effects on the reproductive system and fertility and also fortifying, tonic action and immunomodulating and anti-alergic activity. RJ may cause allergic reactions, asthma and even fatal anaphylaxis in some humans. Therefore, RJ should be orally ingested as nutreaceutical agent or food-ingredient only after an allergy test

Povećanje antioksidacijske aktivnosti ekstrakata dobivenih iz otpada od hrane pomoću β-glukozidaze

Research background. Food by-products such as onion peels and olive leaves are rich in bioactive compounds applicable as natural and low-cost sources of antioxidants. Still, these compounds mainly exist in glycosylated form. Often, hydrolysis of glycoside compounds increases their antioxidant activity and health benefits. However, not many studies have been done concerning the β-glucosidase effect, specifically from Aspergillus niger, on glycosylated compounds within these by-products. Also, changes in the antioxidant activity of the mentioned by-products under the effect of β-glucosidase have not been reported yet. Therefore, this study considers the effect of A. niger β-glucosidase on glucoside compounds and the antioxidant activity of onion peel and olive leaf extracts. Experimental approach. The antioxidant activity of the extracts was determined by 1,1-diphenyl-2-picrylhydrazyl (DPPH) and ferric reducing antioxidant power (FRAP) assays. Also, glucose, total phenolic and flavonoid contents were measured. Moreover, TLC and HPLC analyses were performed before and after the enzymatic hydrolysis. Results and conclusions. The obtained results showed an increase in the extract antioxidant activity after treatment. Also, β-glucosidase increased the glucose content of the extracts. The thin layer chromatography (TLC) and high-performance liquid chromatography (HPLC) results showed the β-glucosidase efficacy to hydrolyze quercetin glucosides in onion peel extract, and the quercetin concentration increased from (0.48±0.04) mg/mL in the untreated extract to (1.26±0.03) mg/mL in the treated extract (0.5% m/V) after 3 h of enzymatic hydrolysis at 45 °C. Also, the content of quercetin-3-O-glucoside increased considerably from (1.8±0.1) to (54±9) µg/mL following the enzyme treatment. Moreover, oleuropein in olive leaf extract (1% m/V) was hydrolyzed completely from (0.382±0.016) to 0 mg/mL by β-glucosidase for 24 h at 50 °C. Novelty and scientific contribution. This study showed that A. niger β-glucosidase, as a stable enzyme, hydrolyzed quercetin and oleuropein glycosides in onion peel and olive leaf extracts. Thus, A. niger β-glucosidase is a good candidate for processing the food waste and extracting valuable bioactive compounds. Also, the treated extracts with higher antioxidant and biological activity, and without bitter taste can be applicable as potent, natural and cost-effective antioxidants in the food industry.Pozadina istraživanja. Otpaci od hrane, kao što su ovojne ljuske luka i lišće masline, bogati su bioaktivnim spojevima koji se mogu primijeniti kao prirodni i jeftini izvor antioksidansa. Ti su spojevi uglavnom prisutni u glikoliziranom obliku. Često se hidrolizom glikozidnih spojeva poveća njihov antioksidacijski učinak i ljekovita svojstva. Međutim, malo je istraživanja o učinku β-glukozidaze, osobito one dobivene iz plijesni Aspergillus niger, na glikozilirane spojeve u tim nusproizvodima prehrambene industrije. Osim toga, dosad nisu objavljeni podaci o utjecaju β-glukozidaze na promjenu njihove antioksidacijske aktivnosti. Stoga je u ovom radu ispitan učinak β-glukozidaze dobivene iz plijesni A. niger na glikozidne spojeve i antioksidacijsku aktivnost ekstrakata iz ljusaka luka i maslinovog lišća. Eksperimentalni pristup. Antioksidacijska aktivnost ekstrakata određena je pomoću metoda DPPH i FRAP. Također, određeni su koncentracija glukoze te ukupni udjeli fenola i flavonoida. Uz to, uzorci su ispitani tankoslojnom kromatografijom (TLC) i tekućinskom kromatografijom visoke djelotvornosti (HPLC) prije i poslije enzimske hidrolize. Rezultati i zaključci. Dobiveni rezultati pokazuju da je nakon obrade enzimom došlo do povećanja antioksidacijske aktivnosti ekstrakata. Osim toga, obrada β-glukozidazom je povećala koncentraciju glukoze u ekstraktu. Rezultati TLC i HPLC analiza potvrdili su učinkovitost β-glukozidaze u hidrolizi kvercetin glukozida iz ekstrakta ljuske luka. Koncentracija se kvercetina povećala s (0,48±0,04) mg/mL u netretiranom uzorku na (1,26±0,03) mg/mL u tretiranom uzorku (0.5 % m/V) nakon 3 sata hidrolize pri 45 °C. Također, udjel se kvercetin-3-O-glukozida nakon tretiranja pomoću enzima bitno povećao s (1,8±0,1) na (54±9) μg/mL. Povrh toga, oleuropein iz ekstrakta lista masline (1 % m/V) u potpunosti je hidroliziran pomoću β-glukozidaze, pa je njegova koncentracija s 0,382±0,016 pala na 0 mg/mL tijekom 24 h pri 50 °C. Novina i znanstveni doprinos. U radu je prikazano da β-glukozidaza, stabilni enzim izoliran iz plijesni A. niger, hidrolizira kvercetin i oleuropein glikozide iz ekstrakata ovojne ljuske luka i maslinovog lišća. Zaključeno je da je β-glukozidaza iz A. niger pogodna za obradu otpada od hrane i ekstrakciju vrijednih bioaktivnih spojeva. Osim toga, dobiveni se ekstrakti s većom antioksidacijskom i biološkom aktivnošću, a koji nemaju gorak okus, mogu primijeniti u prehrambenoj industriji kao jaki, prirodni antioksidansi prihvatljive cijene

Study of antioxidant activity of sheep visceral protein hydrolysate: Optimization using response surface methodology

BACKGROUND: The main objective of this experiment was optimal use of none edible protein source to increase nutritional value of production with high biological function, including antioxidant activity. METHODS: Sheep visceral (stomach and intestine) was used as substrate. Response surface methodology (RSM) was used to optimize hydrolysis conditions for preparing protein hydrolysate from the sheep visceral, using alcalase 2.4 l enzyme. The investigated factors were temperature (43-52 &deg;C), time (90-180 min), and enzyme/substrate ratio (60-90 Anson-unit [AU]/kg protein) to achieve maximum antioxidant activity. Experiments were designed according to the central composite design. RESULTS: Each of the studied variables had a significant effect on responses (P &lt; 0.05). Optimal conditions to achieve antioxidant activity were, temperature (48.27 &deg;C), time (158.78), min and enzyme/substrate ratio (83.35) Anson-unit/kg protein. Under these conditions, antioxidant activity was 68.21%, R2 for model was 0.983. The values indicated the high accuracy of the model to predict the reaction conditions considering different variables. The chemical analysis of protein hydrolysate showed high protein content (83.78%) and low fat content (0.34%). CONCLUSION: Our results showed that protein hydrolysate of sheep visceral, can be used as a natural antioxidant with high nutritional value. &nbsp; Keywords: Antioxidant Peptides, Protein Hydrolysate, Enzyme Hydrolysis, Optimization&nbsp;</p

Peptide identification in alcalase hydrolysated pollen and comparison of its bioactivity with royal jelly

Peptides with a similar antioxidant and ACE-inhibitory activity of royal jelly (RJ) generated from Alcalase hydrolysated pollen (AHP) were predicted by Response Surface Methodology (RSM). The model equations were proposed according to the effects of time and enzyme concentration on the antioxidant and ACE-inhibitory activity. The optimum values for Alcalase concentration and hydrolysis time were 1.5% and 4 h, respectively. Later, AHP was prepared and deproteinised to be further analysed using size-exclusion chromatography (SEC). After SEC separation, fractions with the highest activity of ACE-inhibitory, DPPH radical scavenging and ferric-reducing power were purified by RP-HPLC. The highest ACE-inhibitory and DPPH scavenging activity of fractions was found 100% and 66.61%, respectively. The most active fractions were analysed by nano-liquid chromatography and mass spectrometry in tandem (nLC-MS/MS) and a total of 195 peptide sequences were identified. The origins of all peptides were herbal proteins and certain coincidences with previously described bioactive sequences were discussed.This work was funded by the Ministry of Science, Research and Technology of Iran and the Grant AGL2014-57367-R and FEDER funds from the Spanish Ministry of Economy, Industry and Competitiveness. Ramón y Cajal postdoctoral contract to LM is acknowledged. LC-MS/MS analysis was carried out by in the SCSIE University of Valencia Proteomics Unit (Spain), a member of ISCIII Proteo Red Proteomics Platform

Physicochemical, antioxidant, calcium binding, and angiotensin converting enzyme inhibitory properties of hydrolyzed tomato seed proteins

The objective of this was to determine the impact of enzymatic hydrolysis on the multifunctionality of tomato seed protein hydrolysates (TSPH) and their physicochemical properties. The enzymatic hydrolysis was performed using alcalase and two factors response surface methodology. The best conditions were 131.4 min and 3% enzyme/substrate (E/S) for antioxidant activity; 174.5 min and 2.93% E/S for angiotensin-converting enzyme (ACE) inhibition; and 66.79 min and 2.27% E/S for the calcium binding. Antioxidant and ACE hydrolysates were characterized by higher solubility, zeta potential, and thermal stability while properties of the calcium binding hydrolysate were only minimally affected by the enzymatic hydrolysis. Gel electrophoresis showed that molecular weights of polypeptides in the calcium binding TSPH were higher compared to those in ACE and antioxidant TSPHs. This was due to the low degree of hydrolysis of the calcium binding hydrolysate. Practical applications: Nowadays, different protein sources are used to produce protein hydrolysates containing bioactive peptides that can help alleviate oxidation of foods, oxidative stress, and chronic conditions (e.g., hypertension, diabetes, cardiovascular disorder). Hydrolyzed proteins also have the potential to increase mineral absorption through the formation of mineral-binding complexes.

Controlled enzymatic hydrolysis of pollen protein as promising tool for production of potential bioactive peptides

In the present study, response surface method was used to optimize hydrolysis condition to generate potential bioactive peptides from pollen protein using pepsin (pepsin hydrolysated pollen—PHP) and trypsin (trypsin hydrolysated pollen—THP). Then PHP and THP prepared under optimized conditions were analyzed by size-exclusion chromatography. The fractions possessing the maximum ACE-inhibitory, DPPH radical scavenging, and ferric-reducing power were further purified by RP-HPLC. A heterogeneous composition of hydrophobic and hydrophilic peptides in both fractions was obtained. Finally, peptide sequences in active fractions of PHP and THP were identified by mass spectrometry in tandem. All the identified peptides had herbal protein origins. These were 6–21 amino acids in length, and Glycine and Alanine were two main hydrophobic amino acids present in their sequences. The results proved that using controlled enzymatic hydrolysis of pollen protein is possible to generate bioactive peptides with high ACE-inhibitory and antioxidant activity in final product. Practical applications: Pollen is well-known as an interesting protein source. Compared to other types of hydrolysis, enzymatic hydrolysis of vegetable proteins has few or no undesirable side reactions or products. In this study, controlled enzymatic hydrolysis of pollen protein was applied as a suitable method to produce bioactive peptide. The results proved that using controlled enzymatic hydrolysis of pollen protein is possible to generate bioactive peptides with high ACE-inhibitory and antioxidant activity in final product. This product can be used as functional and health promoting ingredient in different food formulations.This work was financially supported by the Ministry of Science, Research and Technology of Iran, Grant AGL2014‐57367‐R and FEDER funds from the Spanish Ministry of Economy, Industry, and Competitiveness. Ramón y Cajal postdoctoral contract of LM is also acknowledged. MS/MS analysis was conducted in SCSIE University of Valencia Proteomics Unit (Spain) which is registered in ISCIII ProteoRed Proteomics Platform

Impact of Simulated Gastrointestinal Digestion on the Biological Activity of an Alcalase Hydrolysate of Orange Seed (Siavaraze, Citrus sinensis) by-Products

© 2020 by the authors.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.Grant AGL2017-89381-R and FEDER funds from the Spanish Ministry of Economy, Industry and Competitiveness, and Ramón y Cajal postdoctoral contract by L.M. are acknowledged. This work was also supported by Intramural project from CSIC number 201870E006.Peer reviewe