Potential antithrombotic activity detected in amaranth proteins and its hydrolysates

Sabbione, Ana Clara; Scilingo, Adriana Alicia; Añón, Marı́a Cristina

doi:10.1016/j.lwt.2014.07.015

Cited by 66 publications

(53 citation statements)

References 21 publications

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“…In spite of this, Alb1H103 (431.1 ± 0.01 mg/ml) and GloH88 (12.8 ± 0.06 mg/ml) had similar antiplatelet activity of the estrogen Buame (400 lM; Flores-Garcia et al 2012). However, unlike the study by Sabione et al (2015), no inhibition of platelet aggregation with GluH24 was observed. The peptide fraction GluH24 is a hydrolysate that has peptides made up of 3-4 aminoacids (0.45 kDa).…”

Section: Bioactivity Of Amaranth Protein Hydrolysatescontrasting

confidence: 87%

“…Buame (N-(3-hydroxy-1,3,5(10)-estratrien-17b-yl)butylamine), a synthetic estrogen which is a dose-dependant inhibitor on platelet aggregation, induced by ADP, was used as a control. The method used to assess antithrombotic activity was different from the one reported by Sabione et al (2015), which was done using clotting tests such as activated partial thromboplastin time test, prothrombin time test and thrombine time test. They found that albumin (3.8 mg/ml) and globulin (2.5 mg/ml) hydrolysates improved the antithrombotic activity whereas glutelin hydrolysate exhibited the highest antithrombotic activity.…”

Section: Bioactivity Of Amaranth Protein Hydrolysatesmentioning

confidence: 99%

“…They found that albumin (3.8 mg/ml) and globulin (2.5 mg/ml) hydrolysates improved the antithrombotic activity whereas glutelin hydrolysate exhibited the highest antithrombotic activity. Nevertheless it was difficult to compare the concentrations of peptide fractions of amaranth protein hydrolysates with antithrombotic activity in the study by Sabione et al (2015) and present because the trials evaluated different coagulation factors. In spite of this, Alb1H103 (431.1 ± 0.01 mg/ml) and GloH88 (12.8 ± 0.06 mg/ml) had similar antiplatelet activity of the estrogen Buame (400 lM; Flores-Garcia et al 2012).…”

Section: Bioactivity Of Amaranth Protein Hydrolysatesmentioning

confidence: 99%

“…(Dexter and Middelberg 2008). Particularly, storage proteins of amaranth grain, in their primary structure, contain peptides with ACEIA (Fritz et al 2011;, DPPIVIA (Montoya-Rodriguez et al 2015;Velarde-Salcedo et al 2013) and antithrombotic activity (Sabione et al 2015), among others. These bioactivities would be highly relevant in the making of N and FF.…”

Section: Introductionmentioning

confidence: 99%

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Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

et al. 2016

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The aim of this work was to assess the effects of temperature (T), time (t) and pH treatments and an in vitro digestion on the stability of the angiotensin I-convertingenzyme-inhibitory activity (ACEIA) and antithrombotic activity (ATA; assessed as inhibition of platelet aggregation) of selected protein hydrolysates of amaranth named Alb1H103 and GloH88 and GluH24 with dipeptidyl peptidase IV inhibitory activity (DPPIVIA). Heat treatment (40-100°C) for 1 h showed no significant differences among ACEIA, DPPIVIA and ATA of the heated hydrolysates at pH 4 and 7. There was no statistically significant loss of any bioactivity under heat treatment for 3 h at pH 4.0. Alb1H103 and GluH24 maintained the inhibitory activity of ACE and ATA at pH 7.0 for 3 h, whereas GloH88 maintained ACEIA and ATA for 2.0 h at pH 7.0. The pH effect on hydrolysates bioactivity was assessed in the range of 2.0-12.0. This was negligible on ACEIA, ATA and DPPIVIA. The in vitro digestion was performed using pepsin, trypsin (T) and a-chymotrypsin (C). A previous treatment of hydrolysates with pepsin improved the proteolytic activities of T and C. The hydrolysates kept at 100°C for 1 h at pH 4.0, showed a significant increase in bioactivity. Conversely, a treatment at pH 7.0 showed no significant difference (p \ 0.05) in the hydrolysates bioactivities after their digestion. Thus, biological activity of hydrolysates may be preserved or enhanced, depending on their processing conditions.

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Section: Bioactivity Of Amaranth Protein Hydrolysatescontrasting

confidence: 87%

Section: Bioactivity Of Amaranth Protein Hydrolysatesmentioning

confidence: 99%

Section: Bioactivity Of Amaranth Protein Hydrolysatesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

et al. 2016

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“…They have been reported to exhibit a wide range of biological Responsible editor: Philippe Garrigues activity, including antimicrobial, antithrombotic, antioxidative and antihypertensive activities (Balti et al 2015;Sabbione et al 2015;Sila et al 2014a, b;Clare and Swaisgood 2000).…”

Section: Introductionmentioning

confidence: 99%

Valorisation of smooth hound (Mustelus mustelus) waste biomass through recovery of functional, antioxidative and antihypertensive bioactive peptides

Sayari

Sila

Haddar

et al. 2015

Environ Sci Pollut Res

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Concerns over the environmental and waste disposal problems created by the large amounts of by-products generated from fish processing industries are increasing worldwide. The bioconversion of those marine waste by-products through the enzymatic hydrolysis of their protein content offers the possibility for the development of bioactive peptides for use in various biotechnological applications. The present study aimed to investigate and evaluate the biological and functional properties of smooth hound (Mustelus mustelus) protein hydrolysates (SHPHs) obtained by treatment with intestinal and gastric enzyme preparations from M. mustelus viscera and porcine pancreatin. The results revealed that the SHPHs exhibited different degrees of hydrolysis and antioxidant activity. The hydrolysate produced by the intestinal crude extract presented the highest rate of antioxidative activity, showing an IC50 value of 1.47 ± 0.07 mg/mL in 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging assays. The alkaline protease extract from the intestine of M. mustelus produced hydrolysate with the highest angiotensin I-converting enzyme (ACE) inhibitory activity (82 ± 1.52% at 2 mg/mL). All the protein hydrolysates showed excellent solubility and interfacial properties that were governed by pH. The major amino acids detected in SHPHs were glutamic acid/glutamine, aspartic acid/asparagine, histidine and arginine, followed by methionine, phenylalanine, serine, valine and leucine. Overall, the results indicated that smooth hound by-products can be used to generate high value-added products, thus offering a valuable source of bioactive peptides for application in wide range of biotechnological and functional food applications.

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Proteins and Amino Acids of Kernels

et al. 2017

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Potential antithrombotic activity detected in amaranth proteins and its hydrolysates

Cited by 66 publications

References 21 publications

Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

Valorisation of smooth hound (Mustelus mustelus) waste biomass through recovery of functional, antioxidative and antihypertensive bioactive peptides

Proteins and Amino Acids of Kernels

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