Generation of bioactive peptides from lentil protein: degree of hydrolysis, antioxidant activity, phenol content, ACE-inhibitory activity, molecular weight, sensory, and functional properties

Angiotensin I-converting enzyme (ACE) peptides are bioactive peptides that have important value in terms of research and application in the prevention and treatment of hypertension. While widespread literature is concentrated on casein or whey protein for production of ACE-inhibitory peptides, relatively little information is available on selecting the proper proteases to hydrolyze the protein. In this study, skimmed cow and goat milk were hydrolyzed by four commercial proteases, including alkaline protease, trypsin, bromelain, and papain. Angiotensin I-converting enzyme-inhibitory peptides and degree of hydrolysis (DH) of hydrolysates were measured. Moreover, we compared the difference in ACE-inhibitory activity between cow and goat milk. The results indicated that the DH increased with the increase in hydrolysis time. The alkaline protease-treated hydrolysates exhibited the highest DH value and ACE-inhibitory activity. Additionally, the ACE-inhibitory activity of hydrolysates from goat milk was higher than that of cow milk-derived hydrolysates. Therefore, goat milk is a good source to obtain bioactive peptides with ACE-inhibitory activity, as compared with cow milk. A proper enzyme to produce ACE-inhibitory peptides is important for the development of functional milk products and will provide the theoretical basis for industrial production.

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Preparation of rapeseed protein hydrolysates with ACE inhibitory activity by optimization and molecular weight distribution of hydrolysates

Turkish Journal of Biochemistry ◽

10.1515/tjb-2017-0044 ◽

2017 ◽

Vol 42 (4) ◽

Author(s):

Asif Wali ◽

Haile Ma ◽

Muhammad Tayyab Rashid ◽

Qui Fang Liang

Keyword(s):

Molecular Weight ◽

Response Surface ◽

Molecular Weight Distribution ◽

Weight Distribution ◽

Inhibitory Activity ◽

Proteolytic Enzymes ◽

Ace Inhibitory Activity ◽

Rapeseed Protein Hydrolysates ◽

Hydrolysis Conditions ◽

Ace Inhibitory

AbstractObjective:The main purpose of this study was to screen effective proteolytic enzymes for producing hydrolysates from rapes protein, and to optimize hydrolysis conditions using response surface design to prepare hydrolysates with maximum ACE inhibitor activity.Methods:RSM design was successfully applied to the hydrolysis conditions on the basis of single factor experiments which further derived a statistical model for experimental validation. The molecular weight distribution of rapeseed protein hydrolysates with different degree of hydrolysis was also investigated.Results:All the proteolytic enzymes tested produced hydrolysates that possessed ACE inhibitory activity. Aiding RSM design the highest ACE inhibitory activity 56.3% was achieved under optimum hydrolysis conditions at the hydrolysis time, pH, hydrolysis temperature, and enzyme dosage were at 90.11 min, 8.88, 50°C and 3580.36 UgConclusion:Enzymatic hydrolysis and response surface methodology found good techniques in order to achieve hydrolysates with maximum ACE inhibitory activity. The findings of current research suggested that the hydrolysates obtained under optimized conditions could be utilized to formulate nutraceuticals and pharmaceuticals

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Effect ofJatropha curcasPeptide Fractions on the Angiotensin I-Converting Enzyme Inhibitory Activity

BioMed Research International ◽

10.1155/2013/541947 ◽

2013 ◽

Vol 2013 ◽

pp. 1-8 ◽

Cited By ~ 4

Author(s):

Maira R. Segura-Campos ◽

Fanny Peralta-González ◽

Arturo Castellanos-Ruelas ◽

Luis A. Chel-Guerrero ◽

David A. Betancur-Ancona

Keyword(s):

Inhibitory Activity ◽

Protein Hydrolysate ◽

Gel Filtration ◽

Ace Inhibition ◽

Degree Of Hydrolysis ◽

Converting Enzyme ◽

Angiotensin I ◽

Ace Inhibitory Activity ◽

Angiotensin I Converting Enzyme ◽

Ace Inhibitory

Hypertension is one of the most common worldwide diseases in humans. Angiotensin I-converting enzyme (ACE) plays an important role in regulating blood pressure and hypertension. An evaluation was done on the effect of Alcalase hydrolysis of defattedJatropha curcaskernel meal on ACE inhibitory activity in the resulting hydrolysate and its purified fractions. Alcalase exhibited broad specificity and produced a protein hydrolysate with a 21.35% degree of hydrolysis and 34.87% ACE inhibition. Ultrafiltration of the hydrolysate produced peptide fractions with increased biological activity (24.46–61.41%). Hydrophobic residues contributed substantially to the peptides’ inhibitory potency. The 5–10 and <1 kDa fractions were selected for further fractionation by gel filtration chromatography. ACE inhibitory activity (%) ranged from 22.66 to 45.96% with the 5–10 kDa ultrafiltered fraction and from 36.91 to 55.83% with the <1 kDa ultrafiltered fraction. The highest ACE inhibitory activity was observed inF2 ( μg/mL) from the 5–10 kDa fraction andF1 ( μg/mL) from the <1 kDa fraction. ACE inhibitory fractions fromJatrophakernel have potential applications in alternative hypertension therapies, adding a new application for theJatrophaplant protein fraction and improving the financial viability and sustainability of a Jatropha-based biodiesel industry.

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Milk Fermentation by Lacticaseibacillus rhamnosus GG and Streptococcus thermophilus SY-102: Proteolytic Profile and ACE-Inhibitory Activity

Fermentation ◽

10.3390/fermentation7040215 ◽

2021 ◽

Vol 7 (4) ◽

pp. 215

Author(s):

Jessica Lizbeth Sebastián-Nicolas ◽

Elizabeth Contreras-López ◽

Juan Ramírez-Godínez ◽

Alma Elizabeth Cruz-Guerrero ◽

Gabriela Mariana Rodríguez-Serrano ◽

...

Keyword(s):

Molecular Weight ◽

Inhibitory Activity ◽

Ace Inhibition ◽

Added Value ◽

Low Molecular Weight ◽

Ace Inhibitory Activity ◽

Milk Fermentation ◽

Sds Page ◽

Ace Inhibitory

Health benefits of probiotics and production of inhibitors of angiotensin converting enzyme (ACE) released during milk fermentation are well known. That is why in this investigation the proteolytic profile and ACE inhibitory capacity of peptide fractions from protein hydrolysis of milk during fermentation processes was analyzed. Milk fermentation was carried out inoculating 106 CFU of L. rhamnosus GG, S. thermophilus SY-102 and with both bacteria. The proteolytic profile was determined using: TNBS, SDS-PAGE and SEC-HPLC techniques. In vitro ACE inhibition capacity was measured. The pH of 4.5 was reached at 56 h when the milk was fermented with L. rhamnosus, at 12 h with S. thermophillus and at 41 h in the co-culture. Production of free amino groups corresponded with the profile of low molecular weight peptides observed by SDS-PAGE and SEC-HPLC. Co-culture fermentation showed both the highest concentration of low molecular weight peptides and the ACE inhibitory activity (>80%). Results indicated that the combination of lactic cultures could be useful in manufacture of fermented milk with an added value that goes beyond basic nutrition, such as the production of ACE-inhibitory peptides.

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Partial Purification and Characterization of Bioactive Peptides from Cooked New Zealand Green-Lipped Mussel (Perna canaliculus) Protein Hydrolyzates

Foods ◽

10.3390/foods9070879 ◽

2020 ◽

Vol 9 (7) ◽

pp. 879

Author(s):

Ramya Jayaprakash ◽

Conrad O. Perera

Keyword(s):

New Zealand ◽

Inhibitory Activity ◽

Bioactive Peptides ◽

Protein Hydrolysate ◽

Gel Filtration ◽

Partial Purification ◽

Ace Inhibitory Activity ◽

Perna Canaliculus ◽

Inhibitory Activities ◽

Ace Inhibitory

Proteins from fresh New Zealand green-lipped mussels were hydrolyzed for 240 min using pepsin and alcalase. The extent of the hydrolysis, antioxidant, antimicrobial, and angiotensin-converting enzyme (ACE) inhibitory activities of each protein hydrolysate were investigated. Peptides obtained from pepsin hydrolysis after 30 min, named GPH, exhibited the highest antioxidant and ACE inhibitory activity, but no antimicrobial activity. Purification of the GPH using gel-filtration chromatography revealed that the protein fraction (GPH-IV*) containing peptides with a molecular weight (MW) below 5 kDa had the strongest antioxidant and ACE inhibitory activities. Further purification was done using reverse-phase HPLC (RP-HPLC) and the only major peak obtained (GPH-IV*-P2) had the highest antioxidant and ACE inhibitory activity. From this fraction, several bioactive peptides with an MW ≈ 5 kDa were identified using LC-MS and in silico analyses. This research highlights that green-lipped mussel protein hydrolysates could be used as a good source of bioactive peptides with potential therapeutic applications.

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Cheese Whey Fermentation by Its Native Microbiota: Proteolysis and Bioactive Peptides Release with ACE-Inhibitory Activity

Fermentation ◽

10.3390/fermentation6010019 ◽

2020 ◽

Vol 6 (1) ◽

pp. 19 ◽

Cited By ~ 2

Author(s):

Miguel A. Mazorra-Manzano ◽

Glen R. Robles-Porchas ◽

Daniel A. González-Velázquez ◽

María J. Torres-Llanez ◽

Marcel Martínez-Porchas ◽

...

Keyword(s):

Inhibitory Activity ◽

Bioactive Peptides ◽

Cheese Whey ◽

Lactic Acid Production ◽

Whey Proteins ◽

Biological Properties ◽

Effect Of Temperature ◽

Ace Inhibitory Activity ◽

Beneficial Effects ◽

Ace Inhibitory

Cheese whey contains about 20% of the total milk protein and has high nutritional and technological value, as well as attractive biological properties. Whey protein represents an important source of bioactive peptides with beneficial effects on health (e.g., antioxidant, antidiabetic, antihypertensive, etc.). Microbiota in cheese whey can hydrolyze proteins and generate bioactive peptides through a fermentation process. The objective of this study was to evaluate the effect of temperature on the fermentation of cheese whey by its native microbiota, and the action of microbial proteolytic activity on whey proteins to release peptides with inhibitory activity of the angiotensin-converting enzyme (ACE). Whey proteins hydrolysis occurred at all incubation temperatures evaluated (32–50 °C), with the major proteolytic effect within the range of 35–42 °C. Minor whey proteins (i.e., Lf, bovine serum albumin (BSA), and IgG) were more susceptible to degradation, while β-lactoglobulin and α-lactalbumin showed major resistance to microbial proteolytic action. Alfa-amino groups increased from 36 to 360–456 µg Gly/mL after 120 h of fermentation. A higher lactic acid production (11.32–13.55 g/L) and lower pH (3.3–3.5) were also observed in the same temperature range (32–42 °C). In addition, ACE-inhibitory activity increased from 22% (unfermented whey) to 60–70% after 120 h of fermentation. These results suggest that the fermentation of cheese whey by its native microbiota represents an attractive process to give value to whey for the production of whey-based beverages or functional foods with potential antihypertensive properties.

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Insects as source of angiotensin converting enzyme inhibitory peptides

Journal of Insects as Food and Feed ◽

10.3920/jiff2017.0017 ◽

2017 ◽

Vol 3 (4) ◽

pp. 231-240 ◽

Cited By ~ 9

Author(s):

A. Cito ◽

M. Botta ◽

V. Francardi ◽

E. Dreassi

Keyword(s):

Angiotensin Converting Enzyme ◽

Inhibitory Activity ◽

Bioactive Peptides ◽

Hypertension Treatment ◽

Converting Enzyme ◽

Oecophylla Smaragdina ◽

Ace Inhibitory Activity ◽

Inhibitory Peptides ◽

Ace Inhibitory Peptides ◽

Ace Inhibitory

Hypertension is well known as one of the major risk for cardiovascular diseases which annually affect millions of people. The angiotensin converting enzyme (ACE) plays a key role in blood pressure regulation process. Indeed, hypertension treatment by synthetic ACE inhibitors (e.g. captopril, lisinopril and ramipril) is effective; however, their use can cause serious side effects, such as hypotension, cough, reduced renal function and angioedema. Thus, research was focused on natural ACE inhibitory peptides sources such as foodstuffs and also, more recently, edible insects. In the last decades, ACE inhibitory activity has been detected in protein hydrolysates from insect species belonging to the orders of Coleoptera, Diptera, Hymenoptera, Lepidoptera and also Orthoptera. Further investigations led to identify specific ACE inhibitory peptides from the silkworm Bombyx mori (Lepidoptera: Bombycidae), the yellow mealworm Tenebrio molitor (Coleoptera: Tenebrionidae), the cotton leafworm Spodoptera littoralis (Lepidoptera: Noctuidae) and also from the weaver ant Oecophylla smaragdina (Hymenoptera: Formicidae). Even if ACE inhibitory activity of these bioactive peptides has been in vitro assayed and is comparable to those of some bioactive peptides derived from other animal protein sources, the in vivo effectiveness of most of these bioactive peptides still needs to be confirmed. The aim of this review is to present an outline of the currently available data on the potential use of insects for hypertension treatment with a focus on the ACE inhibitory peptides identified in these invertebrates to date.

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Optimisation of the hydrolysis of goat milk protein for the production of ACE-inhibitory peptides

Journal of Dairy Research ◽

10.1017/s0022029913000083 ◽

2013 ◽

Vol 80 (2) ◽

pp. 214-222 ◽

Cited By ~ 7

Author(s):

Francisco Javier Espejo-Carpio ◽

Raúl Pérez-Gálvez ◽

Emilia M Guadix ◽

Antonio Guadix

Keyword(s):

Inhibitory Activity ◽

Milk Protein ◽

Goat Milk ◽

Degree Of Hydrolysis ◽

Ace Inhibitory Activity ◽

Enzyme Substrate ◽

Substrate Ratio ◽

Input Variables ◽

The Individual ◽

Ace Inhibitory

Goat milk protein was hydrolysed with subtilisin and trypsin. As input variables, temperature was assayed in the interval 45–70 °C for subtilisin and 30–55 °C for trypsin, while the enzyme-substrate ratio varied from 1 to 5%. The effect of the input variables on the degree of hydrolysis and ACE-inhibitory activity (output variables) was modelled by second order polynomials, which were able to fit the experimental data with deviations below 10%. The individual maximum values of the degree of hydrolysis and the ACE-inhibitory activity were found at conflicting conditions of temperature and enzyme-substrate ratio. Since such maximum values could not be reached simultaneously, a bi-objective optimisation procedure was undertaken, producing a set of non-inferior solutions that weighted both objectives.

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