Screening of in vitro bioactivities of a soy protein hydrolysate separated by hollow fiber and spiral-wound ultrafiltration membranes

Roblet, Cyril; Amiot, Jean; Lavigne, Charles; Marette, André; Lessard, Martin; Jean, Julie; Ramassamy, Charles; Moresoli, Christine; Bazinet, Laurent

doi:10.1016/j.foodres.2011.11.014

Cited by 41 publications

(14 citation statements)

References 41 publications

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“…It would appear that the 5 min ultrasound‐pretreated sample with 58.23 ± 0.32% relative abundance in this range would be ideal for the generation of bioactive peptides. Ultra‐filtration has been adopted to separate potent from less active peptides, with reported increase in ACE inhibitory activity of 3 kDa permeates when compared to the total hydrolysate.…”

Section: Resultsmentioning

confidence: 61%

“…Increasing the ultrasound pretreatment time up to 5 min increased the peptide relative abundance in the categories 100–500 Da and 500–2000 Da while the 8 min pretreatment had a slightly different distribution of peptides in the 500–2000 Da and 2000–5000 Da of 48.24 ± 0.29% and 42.87 ± 0.20%, respectively. Many bioactive peptides have been found to be within the molecular mass range of 500–3000 Da . It would appear that the 5 min ultrasound‐pretreated sample with 58.23 ± 0.32% relative abundance in this range would be ideal for the generation of bioactive peptides.…”

Section: Resultsmentioning

confidence: 99%

“…33 -35 It would appear that the 5 min ultrasound-pretreated sample with 58.23 ± 0.32% relative abundance in this range would be ideal for the generation of bioactive peptides. Ultra-filtration has been adopted to separate potent from less active peptides, with reported increase in ACE wileyonlinelibrary.com/jsfa inhibitory activity of 3 kDa 33,34 permeates when compared to the total hydrolysate. The 5 min ultrasound-pretreated sample which gave the highest ACE inhibitory activity (0.23 ± 0.09 mg mL −1 ) had the highest molecular mass distribution in the range of 500-2000 Da while the samples pretreated for 8 min had a lower molecular mass distribution in this range and hence a lower ACE inhibitory activity (Table 1).…”

Section: Linking Molecular Mass Distribution With Ace Inhibitionmentioning

confidence: 99%

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Effect of power ultrasound pretreatment on peptidic profiles and angiotensin converting enzyme inhibition of milk protein concentrate hydrolysates

Uluko

Lü

et al. 2014

J Sci Food Agric

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Section: Resultsmentioning

confidence: 61%

Section: Resultsmentioning

confidence: 99%

Section: Linking Molecular Mass Distribution With Ace Inhibitionmentioning

confidence: 99%

See 1 more Smart Citation

Effect of power ultrasound pretreatment on peptidic profiles and angiotensin converting enzyme inhibition of milk protein concentrate hydrolysates

Uluko

Lü

et al. 2014

J Sci Food Agric

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“…Several other studies have shown that bioactive antioxidative peptides are rich in hydrophobic amino acids such as phenylalanine, alanine and proline (Elias, Kellerby, & Decker, 2008). The study conducted by Roblet et al, (2012) by ultrafiltration of soy protein hydrolysates resulted from dual enzymatic hydrolysis (pepsin and pancreatin) produced peptides with relatively high anti oxidative capacity.…”

Section: Introductionmentioning

confidence: 99%

ACE Inhibitory and Antioxidative Bioactive Peptides Derived from Hydrolyzed Soy Milk

Hermanto

Septiana

Putera

et al. 2019

Molekul

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Soy milk is a soybean processed product rich in protein as well as sources of bioactive peptides. Bioactive peptides defined as specific protein fragments that have a positive impact on body functions and conditions and may ultimately influence health. This study was conducted to explore the potential of hydrolyzed soy milk as a source of antioxidative and antihypertensive bioactive peptides through enzymatic hydrolysis. The initial treatment of soy milk protein was acidic precipitation with hydrochloric acid. Furthermore, protein precipitate was hydrolyzed using pepsin proteolytic enzyme with an enzyme: substrate ratio (1:5, 1:10 and 1:20). Protein hydrolysis was carried out for 0–48 hours at 37 °C in an acetate buffer pH 4.5. The soy milk protein hydrolysates were subjected to determination of % DH (Degree of Hydrolysis) and protein profile by SDS-PAGE (sodium dodecyl sulphate polyacrylamide gel electrophoresis). The antihypertensive assay was carried out by in vitro inhibition of the ACE enzyme (Angiotensin Converting Enzyme) and antioxidative activity assay using the DPPH method. The results showed that the optimum conditions for hydrolysis of soy milk were obtained at 40 hours with a % DH value of 53.24% in enzyme ratio 1:20 and the highest antihypertensive activity was obtained from 48 hours hydrolysis with % ACE inhibition value of 79.31%. The highest antioxidative activity of bioactive peptide was obtained at hydrolysis 48 hours with IC50 69.1034 µg / ml. After fractionated and LCMS characterized it was obtained 2 bioactive peptides with molecular weights of 8.954 and 2,696 kDa. These bioactive peptides from hydrolyzed of soymilk might be potential as an antihypertensive agent and reduce oxidative stress.

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“…Glycinin consists of an acid and basic subunits (molecular mass of 34 and 20 KDa respectively), linked together by a disulfide bond, the basic subunit is both hydrophobic and cationic and may be able to react with bacterial cell wall and with acid subunit are responsible for antioxidant and anti-inflammatory activities. 5,6,7,8 Nowadays, consumers are on a constant quest for a younger, prettier, healthier appearances and are seeking alternatives for skin care. This has caught the attention of the cosmetic industry.…”

Section: Introductionmentioning

confidence: 99%

Antimicrobial, antioxidant and anti-inflammatory assessment of a phytocosmetic produced with glycinin peptides

Vasconcellos¹,

Woiciechowski²,

Soccol³

2016

Int J Phytocosmetics Natu Ingredients

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Phytocosmetics are increasingly gaining attention from consumers who search for alternatives for the maintenance and protection of the skin. This article reports formulation of a phytocosmetic derived from defatted soybean flour, an emulsion base that is hydrolyzed from the glycinin protein (1000 µg/g). Test for stability, microbiological control and biological activities antimicrobial (agar diffusion method), antioxidant (method of ABTS/TEAC radicals) and anti-inflammatory (method of hyaluronidase enzyme) properties were conducted. The results indicated that the phytocosmetic was stable and had low indices of microorganisms, according to Resolution 481/99. The bioactivity of the glycinin peptides was not altered or harmed by the other components of the emulsion. For the antimicrobial activity, the bacteria E. coli, S. aureus and P. acnes had values of 30.5 mm, 28 mm and 25 mm halos, respectively. For the antioxidant activity, the result was of 25.1 TEAC and the anti-inflammatory activity was measured at 83.4% inhibition of hyaluronidase enzyme. This study showed that the formulated phytocosmetic has great potential for topical use; it is comparable to other anti-aging cosmetics for daily skin care with antioxidant, anti-inflammatory and antimicrobial properties.

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Screening of in vitro bioactivities of a soy protein hydrolysate separated by hollow fiber and spiral-wound ultrafiltration membranes

Cited by 41 publications

References 41 publications

Effect of power ultrasound pretreatment on peptidic profiles and angiotensin converting enzyme inhibition of milk protein concentrate hydrolysates

Effect of power ultrasound pretreatment on peptidic profiles and angiotensin converting enzyme inhibition of milk protein concentrate hydrolysates

ACE Inhibitory and Antioxidative Bioactive Peptides Derived from Hydrolyzed Soy Milk

Antimicrobial, antioxidant and anti-inflammatory assessment of a phytocosmetic produced with glycinin peptides

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