Psidium Guajava Seed Protein Hydrolysates Exhibit Invitro Antioxidant and Inhibitory activity against a- Amylase and a-Glucosidase

Abstract Prickly ash (Zanthoxylum bungeanum Maxim) seed protein was hydrolyzed with papain to obtain hydrolysates with inhibitory activity against angiotensin-I converting enzyme (ACE). ACE inhibitory peptides (ACEIPs) were successfully purified from seed protein hydrolysates through ultrafiltration and gel chromatography. In vitro ACE inhibitory assay revealed an IC50 value of 0.032± 0.008 mg·mL−1 for a component with <5 kDa molecular weight. Four fractions were isolated by Sephadex G-25 gel chromatography under the following elution conditions: flow rate, 0.6 mL·min−1; initial volume, 2.0 mL; and sample concentration, 30 mg·mL−1. The second fraction showed the highest inhibitory activity with an IC50 value of 0.021±0.007 mg·mL−1. The stability of the ACE inhibitory activity of the obtained ACEIPs was identified under storage conditions with varied temperature, pH, and gastrointestinal protease digestion. Peptides derived from prickly ash seed protein hydrolysates may be a potential resource for exploring functional food or pharmaceuticals against hypertension.

Download Full-text

Angiotensin-I converting enzyme inhibitory activity of Amaranthus hypochondriacus seed protein hydrolysates produced with lactic bacteria and their peptidomic profiles

Food Chemistry ◽

10.1016/j.foodchem.2021.130320 ◽

2021 ◽

pp. 130320

Author(s):

Fabiola Sánchez-López ◽

Víctor J. Robles-Olvera ◽

Madeleine Hidalgo-Morales ◽

Apollinaire Tsopmo

Keyword(s):

Inhibitory Activity ◽

Seed Protein ◽

Protein Hydrolysates ◽

Converting Enzyme ◽

Angiotensin I ◽

Amaranthus Hypochondriacus ◽

Angiotensin I Converting Enzyme ◽

Lactic Bacteria

Download Full-text

Characterization of Protein Hydrolysates from Fish Discards and By-Products from the North-West Spain Fishing Fleet as Potential Sources of Bioactive Peptides

Marine Drugs ◽

10.3390/md19060338 ◽

2021 ◽

Vol 19 (6) ◽

pp. 338

Author(s):

Andreia Henriques ◽

José A. Vázquez ◽

Jesus Valcarcel ◽

Rogério Mendes ◽

Narcisa M. Bandarra ◽

...

Keyword(s):

Inhibitory Activity ◽

Bioactive Peptides ◽

Radical Scavenging Activity ◽

Radical Scavenging ◽

Protein Hydrolysates ◽

Scavenging Activity ◽

North West ◽

Chelating Activity ◽

The North ◽

By Products

Fish discards and by-products can be transformed into high value-added products such as fish protein hydrolysates (FPH) containing bioactive peptides. Protein hydrolysates were prepared from different parts (whole fish, skin and head) of several discarded species of the North-West Spain fishing fleet using Alcalase. All hydrolysates had moisture and ash contents lower than 10% and 15%, respectively. The fat content of FPH varied between 1.5% and 9.4% and had high protein content (69.8–76.6%). The amino acids profiles of FPH are quite similar and the most abundant amino acids were glutamic and aspartic acids. All FPH exhibited antioxidant activity and those obtained from Atlantic horse mackerel heads presented the highest 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, reducing power and Cu2+ chelating activity. On the other hand, hydrolysates from gurnard heads showed the highest ABTS radical scavenging activity and Fe2+ chelating activity. In what concerns the α-amylase inhibitory activity, the IC50 values recorded for FPH ranged between 5.70 and 84.37 mg/mL for blue whiting heads and whole Atlantic horse mackerel, respectively. α-Glucosidase inhibitory activity of FPH was relatively low but all FPH had high Angiotensin Converting Enzyme (ACE) inhibitory activity. Considering the biological activities, these FPH are potential natural additives for functional foods or nutraceuticals.

Download Full-text

Angiotensin I-converting enzyme inhibitory activity of chickpea and pea protein hydrolysates

Food Research International ◽

10.1016/j.foodres.2010.05.003 ◽

2010 ◽

Vol 43 (6) ◽

pp. 1642-1649 ◽

Cited By ~ 66

Author(s):

Chockry Barbana ◽

Joyce Irene Boye

Keyword(s):

Inhibitory Activity ◽

Protein Hydrolysates ◽

Converting Enzyme ◽

Angiotensin I ◽

Pea Protein ◽

Angiotensin I Converting Enzyme

Download Full-text

Amaranth seed protein hydrolysates have in vivo and in vitro antihypertensive activity

Food Chemistry ◽

10.1016/j.foodchem.2010.11.065 ◽

2011 ◽

Vol 126 (3) ◽

pp. 878-884 ◽

Cited By ~ 68

Author(s):

Mariana Fritz ◽

Bruno Vecchi ◽

Gustavo Rinaldi ◽

María Cristina Añón

Keyword(s):

Seed Protein ◽

Protein Hydrolysates ◽

Antihypertensive Activity ◽

Amaranth Seed

Download Full-text

The anti hypertensive nutraceuticals of Vigna sp bean protein hydrolized by alcalase and flavourzyme

Journal of Functional Food and Nutraceutical ◽

10.33555/jffn.v2i1.40 ◽

2020 ◽

Vol 2 (1) ◽

pp. 63-73

Author(s):

Tejasari ◽

Sih Yuwanti ◽

Mohammad Bazar Ahmadi ◽

Yuna Luki Afsari

Keyword(s):

Amino Acids ◽

G Protein ◽

Inhibitory Activity ◽

Protein Hydrolysate ◽

Protein Hydrolysates ◽

Small Molecular Weight ◽

Hydrophobic Amino Acids ◽

Prevention Of Hypertension ◽

Hydrolysis Of ◽

Bean Protein

Peptide with hydrophobic amino acids had been studied for their inhibitory activity against angiotensin-I converting enzyme (ACE-1) transformation into ACE-2 and prevention of hypertension. The active peptides may come from alcalase and flavourzyme hydrolysis of bean protein. This study aimed to measure ACE-1 inhibitory of protein hydrolysates from Vigna sp. bean (mung bean and cowpea) that grew in Indonesia, and its solubility. The bean protein (22.9 - 23.6 %) was extracted using isoelectric precipitation at pH 4-4.6. The extracts were hydrolyzed at pH 8 for alcalase and pH 7 for flavourzyme, followed with inactivation at 80-85 oC. ACE-1 inhibitory activity was calculated based on the amount of hippuric acid (HA) formed by the hydrolysis of Hippuryl-His-Leu (HHL), in spectrophotometry detection method (228 nm). Ultrachromatography evaluation showed that the protein hydrolysates of mungbean contained higher hydrophobic amino acids (382 mg/g protein) compared to those of cowpea (329 mg/g protein). Protein hydrolysates of both beans from alcalase hydrolysis have higher ACE-1 inhibitory activity rather than those from flavourzyme. Protein hydrolysate from Vigna spp bean protein hydrolysis by alcalase, contained small molecular weight peptides (3.9-4.63 kDa) and high ACE-1 inhibition ability (80-93 %), and therefore suggested as antihypertensive nutraceuticals. Highest solubility of protein hydrolysates resulted from alcalase hydrolysis of both beans were observed at pH 8, while those resulted from flavorzyme hydrolysis were at pH 7, respectively.

Download Full-text

Functional coix seed protein hydrolysates as a novel agent with potential hepatoprotective effect

Food & Function ◽

10.1039/d0fo01658f ◽

2020 ◽

Vol 11 (11) ◽

pp. 9495-9502

Author(s):

Li-Chun Chen ◽

Shi-Yu Zhang ◽

Yu Zi ◽

Hui-Min Zhao ◽

Hong-Yu Wang ◽

...

Keyword(s):

Liver Injury ◽

Seed Protein ◽

Protein Hydrolysates ◽

Hepatoprotective Effect ◽

Coix Seed ◽

Underlying Mechanisms ◽

Novel Agent

The aim of this study is to explore the hepatoprotective potential of coix seed protein hydrolysates (CPP) against alcohol-induced liver injury, and investigate the underlying mechanisms.

Download Full-text