scholarly journals Trends in valorization of the invasive crab Portunus segnis for cleaner production of chitin, chitosan, and protein hydrolysate

2021 ◽  
Author(s):  
Fadoua Jabeur ◽  
Sondes Mechri ◽  
Fethi Mensi ◽  
Ines Gharbi ◽  
Yosri Ben Naser ◽  
...  
Keyword(s):  
Blue Crab ◽  
Protein Hydrolysate ◽  
Radical Scavenging ◽  
Angiotensin I Converting Enzyme ◽  
Chitin And Chitosan ◽  
Recalcitrant Waste ◽  
Product Powder ◽  
Anoxybacillus Kamchatkensis ◽  
Portunus Segnis ◽  
Central Composite

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 invasive blue crab Portunus segnis bio-waste. Optimization of proteases production was performed 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 recovered protein hydrolysate (P Hyd ) was found to be active towards radical scavenging power, and against angiotensin I-converting enzyme (ACE). The extraction efficiency of the blue crab chitin (BC) 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%. The spectrum of chitin and chitosan were depicted by Fourier-transform infrared spectroscopy (FTIR). The biological value of Pspp and its obtained derivates were evidenced via accredited protocols. These data constitute a roadmap towards a circular and sustainable bio-economic strategy for a clean transformation of a recalcitrant waste to bio-based products.

scholarly journals Extraction and Characterization of Chitin, Chitosan, and Protein Hydrolysate From the Invasive Pacific Blue Crab, Portunus Segnis (Forskål, 1775) Having Potential Biological Activities

2021 ◽  
Author(s):  
Fadoua Jabeur ◽  
Sondes Mechri ◽  
Fethi Mensi ◽  
Ines Gharbi ◽  
Yosri Ben Naser ◽  
...  
Keyword(s):  
Blue Crab ◽  
Pathogenic Bacteria ◽  
Protein Hydrolysate ◽  
Biological Activities ◽  
Radical Scavenging ◽  
Angiotensin I Converting Enzyme ◽  
Product Powder ◽  
Anoxybacillus Kamchatkensis ◽  
Portunus Segnis

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.

scholarly journals Angiotensin-I-Converting Enzyme Inhibitory and Antioxidant Activities of Protein Hydrolysate from Muscle of Barbel (Barbus callensis)

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Assaad Sila ◽  
Anissa Haddar ◽  
Oscar Martinez-Alvarez ◽  
Ali Bougatef
Keyword(s):  
Antioxidant Activities ◽  
Muscle Protein ◽  
Protein Hydrolysate ◽  
Radical Scavenging ◽  
Reducing Power ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

The present study investigated angiotensin-I-converting enzyme (ACE) inhibitory and antioxidant activities of barbel muscle protein hydrolysate prepared with Alcalase. The barbel muscle protein hydrolysate displayed a high ACE inhibitory activity (CI50=0.92 mg/mL). The antioxidant activities of protein hydrolysate at different concentrations were evaluated using variousin vitroantioxidant assays, including 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical method and reducing power assay. The barbel muscle protein hydrolysate exhibited an important radical scavenging effect and reducing power. These results obtained byin vitrosystems obviously established the antioxidant potency of barbel hydrolysate to donate electron or hydrogen atom to reduce the free radical. Furthermore, these bioactive substances can be exploited into functional foods or used as source of nutraceuticals.

scholarly journals Characterization, Bioactivity and Application of Chitosan-Based Nanoparticles in a Food Emulsion Model

Polymers ◽  
2021 ◽  
Vol 13 (19) ◽  
pp. 3331
Author(s):  
Karina Oliveira Lima ◽  
Cristian Mauricio Barreto Pinilla ◽  
Ailén Alemán ◽  
M. Elvira López-Caballero ◽  
M. Carmen Gómez-Guillén ◽  
...  
Keyword(s):  
Food System ◽  
Protein Hydrolysate ◽  
Radical Scavenging Activity ◽  
Chitosan Nanoparticles ◽  
Radical Scavenging ◽  
Physicochemical Characteristics ◽  
Angiotensin I Converting Enzyme ◽  
Bioactive Properties ◽  
Emulsion Model ◽  
Food Applications

In this study, chitosan nanoparticles (CNPs) were prepared by the ionic gelation technique with tripolyphosphate (TPP), and the effect of CNP composition and physicochemical characteristics were evaluated. After the synthesis optimization, CNPs were used as carriers for a fish protein hydrolysate (FPH) with bioactive properties (CNPH). The physicochemical characteristics, antioxidant capacity and antimicrobial, antihypertensive and emulsifier properties of unloaded and loaded CNPs in a food system model were studied. CNPH showed a uniform particle distribution, size ~200 nm, high stability (zeta potential around 30 mV), radical scavenging activity and increased antimicrobial activity against Staphylococcus aureus, Shigella sonnei and Aeromonas hydrophila. Additionally, CNPH showed an angiotensin I-converting enzyme (ACE)-inhibitory activity of 63.6% and, when added to a food emulsion model, this system containing CNPs, with or without FHP, exhibited improved food emulsion stability. Thus, CNPs were able to carry the FPH while maintaining their bioactive properties and can be an alternative to the delivery of bioactive peptides with potential as an emulsion stabilizer for food applications.

scholarly journals Optimized green extraction conditions of matcha green tea (Camellia sinensis) using central composite design for maximal polyphenol and antioxidant contents

BioResources ◽  
2021 ◽  
Vol 16 (2) ◽  
pp. 3255-3271
Author(s):  
Nor Hafiza Sayuti ◽  
Ammar Akram Kamarudin ◽  
Norazalina Saad ◽  
Nor Asma Ab. Razak ◽  
Norhaizan Mohd Esa
Keyword(s):  
Central Composite Design ◽  
Green Tea ◽  
Camellia Sinensis ◽  
Desirability Function ◽  
Radical Scavenging ◽  
Antioxidant Compounds ◽  
Green Extraction ◽  
Antioxidant Content ◽  
Optimum Extraction ◽  
Central Composite

Response surface methodology (RSM) was employed to optimize the extraction conditions of phenolic and antioxidant compounds from matcha green tea (Camellia sinensis) using central composite design (CCD). The desirability function was used to find the optimum extraction conditions. The highest polyphenol and antioxidant content yield were reached at a temperature of 80 °C, an extraction time of 20 min, a liquid-to-solid ratio of 100 mL/g, and a desirability value of 0.948. The experimental values for total phenolics under the optimum extraction conditions were 317.62 ± 3.45 mg GAE/g and 29.21 ± 0.38 mg RE/g for the total flavonoids. The antioxidant activity (AA) was evaluated using 2,2 diphenyl-1-picrylhydrazyl (DPPH) and 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), which showed radical scavenging activities at 88.28 ± 0.14% and 90.02 ± 0.14%, respectively. The high performance liquid chromatography (HPLC) analysis at the optimum condition revealed 14 compounds. Among the analyzed compounds, matcha green tea extract (MGTE) had the highest content of epigallocatechin gallate (EGCG) with 95.48 mg/g, followed by epicatechin gallate (ECG) at 74.48 mg/g, and catechin at 28.94 mg/g. The results suggested that the optimized parameters of heat-assisted extraction provide an ideal green extraction method for the extraction of the high polyphenol and antioxidant content in matcha green tea.

scholarly journals Antioxidant and antihypertensive activities of wonderful cola (Buchholzia coriacea) seed protein and enzymatic protein hydrolysates

2018 ◽  
Vol 3 ◽  
pp. 133-143 ◽  
Author(s):  
Oluwole S. Ijarotimi ◽  
Sunday A. Malomo ◽  
Adeola M. Alashi ◽  
Ifeanyi D. Nwachukwu ◽  
Tayo N. Fagbemi ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Protein Hydrolysate ◽  
Antioxidant Properties ◽  
Radical Scavenging ◽  
Protein Isolate ◽  
Active Inhibitor ◽  
Spontaneously Hypertensive ◽  
Reducing Ability ◽  
Peptide Fractions

The aim of this work was to produce wonderful cola protein hydrolysate fractions with in vitro antioxidant properties coupled with blood pressure-reducing ability when orally administered to spontaneously hypertensive rats (SHRs). Wonderful cola protein isolate (WCI) was hydrolyzed with pancreatin to produce a hydrolysate (WCH), which was subjected to ultrafiltration separation using 1, 3, 5, and 10 kDa molecular weight cut-off membranes to obtain <1, 1–3, 3–5 and 5–10 kDa peptide fractions, respectively. The <1 and 1–3 kDa fractions had higher contents of arginine when compared to the 3–5 and 5–10 kDa peptides. The WCH and <1 kDa peptide fraction had significantly (p < 0.05) better DPPH radical scavenging (55–67%) and metal chelation (83–93%) activities but lower hydroxyl radical scavenging power (10–32%) than the WCI (46, 46 and 63%, respectively). The <1 kDa had significantly (p < 0.05) higher in vitro inhibition (80%) of angiotensin converting enzyme (ACE) activity while the 5–10 kDa was the most active inhibitor (90%) of renin activity. All peptide fractions so produced had better systolic and diastolic blood pressure-lowering effects than WCH and WCI. However, the <1 kDa fraction produced significantly (p < 0.05) stronger systolic (−33 mmHg) and diastolic (−30 mmHg) blood pressure reductions 6 h after oral gavage to SHRs. Thus, wonderful cola proteins contain encrypted bioactive peptides that may be used to formulate antioxidant and antihypertensive products.

scholarly journals Antioxidant Peptides from the Protein Hydrolysate of Spanish Mackerel (Scomberomorous niphonius) Muscle by in Vitro Gastrointestinal Digestion and Their in Vitro Activities

Marine Drugs ◽  
2019 ◽  
Vol 17 (9) ◽  
pp. 531 ◽  
Author(s):  
Zhao ◽  
Yang ◽  
Wang ◽  
Zhao ◽  
Chi ◽  
...  
Keyword(s):  
Protein Hydrolysate ◽  
Radical Scavenging ◽  
Model Systems ◽  
Dpph Radical ◽  
Antioxidant Peptides ◽  
Gastrointestinal Digestion ◽  
Spanish Mackerel ◽  
In Vitro Gastrointestinal Digestion ◽  
Dpph Radical Scavenging

For the full use of Spanish mackerel (Scomberomorous niphonius) muscle to produce antioxidant peptides, the proteins of Spanish mackerel muscle were separately hydrolyzed under five kinds of enzymes and in vitro gastrointestinal digestion, and antioxidant peptides were isolated from the protein hydrolysate using ultrafiltration and multiple chromatography methods. The results showed that the hydrolysate (SMPH) prepared using in vitro GI digestion showed the highest degree of hydrolysis (27.45 ± 1.76%) and DPPH radical scavenging activity (52.58 ± 2.68%) at the concentration of 10 mg protein/mL among the six protein hydrolysates, and 12 peptides (SMP-1 to SMP-12) were prepared from SMPH. Among them, SMP-3, SMP-7, SMP-10, and SMP-11 showed the higher DPPH radical scavenging activities and were identified as Pro-Glu-Leu-Asp-Trp (PELDW), Trp-Pro-Asp-His-Trp (WPDHW), and Phe-Gly-Tyr-Asp-Trp-Trp (FGYDWW), and Tyr-Leu-His-Phe-Trp (YLHFW), respectively. PELDW, WPDHW, FGYDWW, and YLHFW showed high scavenging activities on DPPH radical (EC50 1.53, 0.70, 0.53, and 0.97 mg/mL, respectively), hydroxyl radical (EC50 1.12, 0.38, 0.26, and 0.67 mg/mL, respectively), and superoxide anion radical (EC50 0.85, 0.49, 0.34, and 1.37 mg/mL, respectively). Moreover, PELDW, WPDHW, FGYDWW, and YLHFW could dose-dependently inhibit lipid peroxidation in the linoleic acid model system and protect plasmid DNA (pBR322DNA) against oxidative damage induced by H2O2 in the tested model systems. In addition, PELDW, WPDHW, FGYDWW, and YLHFW could retain their high activities when they were treated under a low temperature (<60 °C) and a moderate pH environment (pH 5–9). These present results indicate that the protein hydrolysate, fractions, and isolated peptides from Spanish mackerel muscle have strong antioxidant activity and might have the potential to be used in health food products.

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