Application of amaranth protein isolate and hydrolysate on a reduced salt fish restructured product: antioxidant properties, textural and microbiological effects

2015 ◽  
Vol 50 (6) ◽  
pp. 1452-1460 ◽  
Author(s):  
Susan F. García Fillería ◽  
Valeria A. Tironi
Foods ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 2297
Author(s):  
Alvaro Villanueva-Lazo ◽  
Sergio Montserrat-de la Paz ◽  
Noelia Maria Rodriguez-Martin ◽  
Francisco Millan ◽  
Cecilio Carrera ◽  
...  

Twelve high-quality chia protein hydrolysates (CPHs) were produced from chia protein isolate (CPI) in a pilot plant of vegetable proteins. To obtain functional hydrolysate, four CPHs were hydrolyzed by the action of Alcalase, an endoprotease, and the other eight CPHs were hydrolyzed by the action of Flavourzyme, an exoprotease. Alcalase-obtained CPHs showed significant antihypertensive properties particularly, the CPH obtained after 15 min of hydrolysis with Alcalase (CPH15A), which showed a 36.2% hydrolysis degree. In addition, CPH15A increased the antioxidant capacity compared to CPI. The CPH15A physicochemical composition was characterized and compared to chia defatted flour (CDF) and CPI, and its techno-functional properties were determined by in vitro experiments through the analysis of its oil absorption capacity, as well as the capacity and stability of foaming and emulsifying, resulting in an emulsifier and stabilizer better than the intact protein. Therefore, the present study revealed that CPH15A has potent antihypertensive and antioxidant properties and can constitute an effective alternative to other plant protein ingredients sources that are being used in the food industry.


2018 ◽  
Vol 3 ◽  
pp. 133-143 ◽  
Author(s):  
Oluwole S. Ijarotimi ◽  
Sunday A. Malomo ◽  
Adeola M. Alashi ◽  
Ifeanyi D. Nwachukwu ◽  
Tayo N. Fagbemi ◽  
...  

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.


Heliyon ◽  
2018 ◽  
Vol 4 (10) ◽  
pp. e00877 ◽  
Author(s):  
Taiwo Ayodele Aderinola ◽  
Tayo Nathaniel Fagbemi ◽  
Victor Ndigwe Enujiugha ◽  
Adeola Monisola Alashi ◽  
Rotimi Emmanuel Aluko

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Ruann Janser Soares de Castro ◽  
Helia Harumi Sato

This study reports the biochemical characterization of a protease from Aspergillus oryzae LBA 01 and the study of the antioxidant properties of protein hydrolysates produced with this protease. The biochemical characterization showed that the enzyme was most active over the pH range 5.0–5.5 and was stable from pH 4.5 to 5.5. The optimum temperature range for activity was 55–60°C, and the enzyme was stable at temperatures below 45°C. The activation energy (Ea) for azocasein hydrolysis and temperature quotient (Q10) were found to be 37.98 kJ mol−1 and 1.64–1.53 at temperature range from 30 to 55°C, respectively. The enzyme exhibited t1/2 of 97.63 min and a D value of 324.31 at the optimum temperature for activity (57.2°C). Protease from A. oryzae LBA 01 was shown as a potentially useful biocatalyst for protein hydrolysis, increasing the antioxidant activities of soy protein isolate, bovine whey protein, and egg white protein from 2.0- to 10.0-fold.


2019 ◽  
Vol 37 (No. 4) ◽  
pp. 260-267 ◽  
Author(s):  
Katarzyna Skrzypczak ◽  
Bartosz Sołowiej ◽  
Adam Waśko ◽  
Anna Kononiuk ◽  
Waldemar Gustaw

The investigation determined the influence of Lactobacillus helveticus strains (T80, T105, B734 and DSMZ 20075) and Lactobacillus acidophilus La-05 (probiotic strain) on the antioxidant activity of whey and milk protein preparations. In order to indicate possible mechanism of antioxidant activity of the obtained hydrolysates, the reducing power (RP) assay, ability to neutralize free radicals and Fe2+ chelating activity analysis were employed. The results suggest that antioxidant activity of tested hydrolysates depends on the type of protein preparation (substrate) and the applied bacterial strain. The strongest antioxidant activity was exhibited by whey protein isolate hydrolysate obtained by using L. helveticus T80. A majority of fermented products obtained with the use of the probiotic strain were characterized by higher antioxidant properties than those obtained by application of L. helveticus. The solution of caseinoglicomacropeptide fermented by strain T105 exhibited the highest RP values, while α-lactalbumin hydrolysed by probiotic strain (La-5) was characterized by the strongest Fe2+ chelating activity. The analysed protein preparations and their hydrolysates obtained with using tested bacteria might potentially be applied in food products in order to inhibit oxidation processes.


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