Antihypertensive Hydrolysates Research Articles

Soybean-derived antihypertensive hydrolysates attenuate Ang II-induced renal damage by modulating MAPK and NF-κB signaling pathways.

Hypertension-induced kidney injury is considered a vital consequence of long-term and uncontrolled hypertension, which is commonly associated with an excessive accumulation of angiotensin II (Ang II) from hyperactivated RAS. Antihypertensive peptides have a significant effect on blood pressure regulation, but few studies have focused on the ameliorative function of antihypertensive peptides on renal injury. This study explored the effects of soybean protein-derived hydrolysate (SPH) on SHR and Ang II-induced HK-2 cells. SPH significantly attenuated blood pressure and alleviated renal pathological injury in SHRs after oral gavage administration. According to the pathological results, the kidneys of SHRs showed inflammation and SPH attenuated inflammatory cell infiltration in the kidneys of SHRs. Immunohistochemical analysis further revealed that SPH inhibited MCP-1 expression and increased Nrf2 expression in the kidneys. An in vitro HK-2 cell model demonstrated that SPH exhibited optimal activity for reducing Ang II-induced inflammatory cytokines and ROS overproduction. Mechanistically, SPH was observed to regulate MAPK/JNK and NF-κB signaling pathways. These findings indicate that potent antihypertensive SPH significantly ameliorates hypertension-induced kidney damage.

Antioxidant and angiotensin-I-converting enzyme (ACE-I) inhibitory activities of protein hydrolysates derived from water buffalo (Bubalus bubalis) liver.

In the current study, we attempted to use ginger as a novel and natural source of protease in comparison with other commercially available enzymes to extract and characterize antioxidant and antihypertensive hydrolysates from water buffalo liver, a protein rich offal. Hydrolysis of protein extracts from buffalo liver using proteinase-K, pronase-E and ginger protease significantly increased the %degree of hydrolysis (18.5-55%) and generated low-molecular weight peptides evident from SDS-PAGE. Enzyme treated hydrolysates exhibited higher (p < 0.05) DPPH radical scavenging activity (43.7-82.4%) and angiotensin-I-converting enzyme (ACE-I) inhibitory activity (46.9-50.1%) relative to control. Mass spectrometric analysis (MALDI-TOF MS) of selected gel-filtered fractions identified few important peptides derived from nuclear ribonucleoprotein, pyruvate kinase and phosphoglycerate kinase that possess strong antioxidant activity. Present findings indicate the efficacy of partially purified ginger as a novel source of protease in generating protein hydrolysates from water buffalo liver with significant antioxidant and antihypertensive activity in vitro. We successfully demonstrated the recovery of functional bioactive peptides from water buffalo liver which presents a potential opportunity for the meat industries to economically use this important byproduct.

Recently isolated food-derived antihypertensive hydrolysates and peptides: A review

Hypertension is a non-communicable disease characterized by elevated blood pressure, and a prominent metabolic syndrome of modern age. Food-borne bioactive peptides have shown considerable potencies as suitable therapeutic agents for hypertension. The peptide inhibition of the angiotensin I-converting enzyme (ACE) from its default biochemical conversion of Ang I to Ang II has been studied and more relatively adopted in several studies. This review offers an examination of the isolation of concomitant proteins in foods, their hydrolysis into peptides and the biofunctionality checks of those peptides based on their anti-hypertensive potentialities. Furthermore, critical but concise details about methodologies and analytical techniques used in the purification of such peptides are discussed. This review is a beneficial literature supplement for scholars and provides functional awareness material for the food-aligned alternative therapy for hypertension. In addition, it points researchers in the direction of adopting food materials and associated by-products as natural sources for the isolation biologically active peptides.

Multifunctional hydrolysates from kenaf (Hibiscus cannabinus L.) seed protein with high antihypertensive activity in vitro and in vivo

Kenaf (Hibiscus cannabinus L.) seed is an underutilized protein-rich resource considered as a by-product of the kenaf fiber processing industry. Its high protein content (34%) makes it a promising candidate as a source of bioactive protein hydrolysates. In this study, the potential of enzymatically hydrolyzed kenaf seed protein to generate multifunctional bioactive peptides was evaluated. Kenaf seed protein concentrate was hydrolyzed using four different proteolytic enzymes (papain, alcalase, bromelain, and flavourzyme) at their respective optimum pH and temperature. The choice of enzyme affected the bioactivities to a certain degree as KSPH were shown to possess high ACE inhibitory activity and low-to-moderate DPP-IV and antioxidant activity. Papain KSPH showed the highest ACE inhibitory activity with 95% inhibition compared to other enzymatic hydrolysates, and therefore was chosen for further investigation of its antihypertensive activity. Papain KSPH was profiled for its hydrophobicity by RP-HPLC and revealed that the majority of late-eluting fractions exerted the highest ACE inhibitory activity. Spontaneously hypertensive rats showed a decrease of approximately 18–46 mmHg in their systolic blood pressure (BP) from 0 to 24 h after oral administration of papain KSPH at dosages of 100 mg/kg, 300 mg/kg, and 500 mg/kg. However, the effect was not dose-dependent. As a novel protein source, future research should aim to demonstrate the safety of kenaf seed protein and its hydrolysates, and validate its bioactivity through human intervention trials. Overall, kenaf seed protein has the potential to generate antihypertensive hydrolysates with multifunctional bioactivities as part of a functional food ingredient.

Antioxidant and antihypertensive hydrolysates obtained from by-products of cannery sardine and brewing industries

abstractHydrolysates with antioxidant and antihypertensive activities were obtained from sarcoplasmic proteins of canned sardine by-product and proteases extracted from Brewer’s spent yeast. Using response surface methodology, hydrolysis time and temperature were selected to achieve the maximum bioactivity. Hydrolysates produced using the substrate/enzyme ratio 1:0.27 (mg/U), 7 h and 50ºC, presenting an angiotensin I-converting enzyme-inhibitory activity of 164 µg protein/mL and an antioxidant activity of 293 μM TE/mL. Experimental results agreed with predicted values within a 95% confidence interval. Within this work the simultaneous valorisation of two agro-industrial by-products was successfully achieved.

Dairy yeasts produce milk protein-derived antihypertensive hydrolysates

The potential of 20 dairy yeast strains belonging to Debaryomyces hansenii, Kluyveromyces lactis and Kluyveromyces marxianus species was examined for the production of milk protein-derived antihypertensive hydrolysates. For this purpose yeast strains were grown in microbiological medium with casein or lactoferrin as sole nitrogen source, and the inhibitory effects of casein and lactoferrin hydrolysates (CSHs and LFHs) on angiotensin I-converting enzyme (ACE) activity were determined. Based on the ACE-inhibitory activity, four CSHs and five LFHs were selected, and permeate fractions with molecular masses lower than 3kDa (pCSHs and pLFHs) were obtained. In vitro ACE-inhibitory potencies (IC50) of permeates varied from 18.8 to 87.6μg/ml (pCSHs) and from 50.2 to 500μg/ml (pLFHs). K. marxianus Km2 strain grown on either casein or lactoferrin produced the most potent permeates. pCSHs and pLFHs were orally administered to spontaneously hypertensive rats (SHRs) and exerted in vivo antihypertensive effect. In conclusion, the present study contributes to a better insight into bioactive compounds produced by dairy yeasts and shows the feasibility of selected yeasts to produce orally effective antihypertensive milk protein-derived hydrolysates.

Sodium Caseinate 가수분해물의 Angiotensin-I Converting Enzyme 저해효과에 관한 연구

This study was carried out to identify the ACE (Angiotensin converting enzyme) inhibitory activity of casein hydrolysates for development of anti-hypertensive hydrolysates. Sodium caseinate was treated with six kinds of commercial proteases such as Flavourzyme, Protamex, Neutrase 1.5, Alcalase, Protease M, and Protease S for 8 h individually, and was then treated with the enzyme combination for 4 h at 45 o C. The hydrolysate which had the highest ACE inhibitory effect was then hydrolysed successively with three digestive enzymes: pepsin, trypsin, and α-chymotrypsin, at 37 o C for 4 h under conditions mimicking those of the gastrointestinal tract. UF (ultra filtration) treatment was applied to one of the secondary hydrolysates to determine ACE inhibitory activity. When sodium caseinate was hydrolysed by commercial proteases, the degree of hydrolysis (DH) showed 2.54 to 4.25% and after secondary hydrolysis, DH showed 4.30 to 5.22%. ACE inhibitory activity and IC50 values decreased, and inhibition rates increased during hydrolysis. Protamex treatment showed the lowest IC50 value (516 µg/mL) and Flavourzyme hydrolysate showed the highest IC50 value (866 µg/mL). As the first hydrolysate was treated with Flavourzyme, the ACE inhibitory activity increased. Neutrase hydrolysate had the highest activity with an IC50 value (282 µg/mL). When Neutrase plus Flavourzyme treatment was hydrolyzed by digestive enzymes, the IC50 value (597 µg/mL) was decreased statistically (p<0.05). As Neutrase plus Flavourzyme hydrolysate is treated by UF with MW cut-off 10,000, permeate showed 273 µg/mL of IC50 value, showed no difference, but retentate which has over MW 10,000 showed statistically different IC50 value, 635 µg/mL (p<0.05).

Production, in continuous enzymatic membrane reactor, of an anti-hypertensive hydrolysate from an industrial alfalfa white protein concentrate exhibiting ACE inhibitory and opioid activities

A few hydrolysates of food proteins were reported to exert an antihypertensive effect in vivo due to angiotensin I converting enzyme (ACE) inhibitory peptides or opioid peptides. An industrial alfalfa white protein concentrate (AWPC) hydrolysate, produced on a pilot plant scale, strongly inhibited ACE with an IC50 value of 8.8 μg/ml. Furthermore, the AWPC hydrolysate inhibited the spontaneous contraction of rabbit ileum in a dose-dependent and naloxone-blocked manner, indicating the presence of opioid peptides. The AWPC hydrolysate significantly lowered blood pressure of spontaneously hypertensive rats (SHR) more than 6 h after a single oral administration. The maximum reduction of systolic blood pressure (−29.9 ± 2.0 mmHg) was observed 4 h after an oral administration of 0.5 g/kg hydrolysate dosage. The minimal anti-hypertensive effect was observed for 0.1 g/kg dosage. The AWPC hydrolysate may then be particularly suitable as nutraceutical for functional food useful in the prevention of hypertension.