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

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

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

Fermentation ◽  
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.

scholarly journals A novel angiotensin I-converting enzyme inhibitory peptide derived from the trypsin hydrolysates of salmon bone proteins

PLoS ONE ◽  
2021 ◽  
Vol 16 (9) ◽  
pp. e0256595
Author(s):  
Thanakrit Kaewsahnguan ◽  
Sajee Noitang ◽  
Papassara Sangtanoo ◽  
Piroonporn Srimongkol ◽  
Tanatorn Saisavoey ◽  
...  
Keyword(s):  
Response Surface ◽  
Inhibitory Activity ◽  
Fish Bone ◽  
Protein Hydrolysates ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

When fish are processed, fish bone becomes a key component of the waste, but to date very few researchers have sought to use fish bone to prepare protein hydrolysates as a means of adding value to the final product. This study, therefore, examines the potential of salmon bone, through an analysis of the benefits of its constituent components, namely fat, moisture, protein, and ash. In particular, the study seeks to optimize the process of enzymatic hydrolysis of salmon bone with trypsin in order to produce angiotensin-I converting enzyme (ACE) inhibitory peptides making use of response surface methodology in combination with central composite design (CCD). Optimum hydrolysis conditions concerning DH (degree of hydrolysis) and ACE-inhibitory activity were initially determined using the response surface model. Having thus determined which of the salmon bone protein hydrolysates (SBPH) offered the greatest level of ACE-inhibitory activity, these SBPH were duly selected to undergo ultrafiltration for further fractionation. It was found that the greatest ACE-inhibitory activity was achieved by the SBPH fraction which had a molecular weight lower than 0.65 kDa. This fraction underwent further purification using RP-HPLC, revealing that the F7 fraction offered the best ACE-inhibitory activity. For ACE inhibition, the ideal peptide in the context of the F7 fraction comprised eight amino acids: Phe-Cys-Leu-Tyr-Glu-Leu-Ala-Arg (FCLYELAR), while analysis of the Lineweaver-Burk plot revealed that the FCLYELAR peptide can serve as an uncompetitive ACE inhibitor. An examination of the molecular docking process showed that the FCLYELAR peptide was primarily able to provide ACE-inhibitory qualities as a consequence of the hydrogen bond interactions taking place between ACE and the peptide. Furthermore, upon isolation form the SBPH, the ACE-inhibitory peptide demonstrated ACE-inhibitory capabilities in vitro, underlining its potential for applications in the food and pharmaceutical sectors.

Optimization of Ultrasonic Wave Extraction Technology of Polysaccharides from Auricularia auricula by Response Surface Methodology and Molecular Weight Distributions

2011 ◽  
Vol 183-185 ◽  
pp. 1852-1858
Author(s):  
Xin Zhao ◽  
Fang Zhou ◽  
Lei Zhu ◽  
Zhen Yu Wang
Keyword(s):  
Molecular Weight ◽  
Response Surface Methodology ◽  
Response Surface ◽  
Ultrasonic Wave ◽  
Molecular Weight Distribution ◽  
Weight Distribution ◽  
Extraction Time ◽  
Extraction Technology ◽  
Auricularia Auricula ◽  
Two Factors

In order to optimize the ultrasonic wave extraction technique of polysaccharides from Auricularia auricula, the technique conditions were carried out by response surface methodology. Then the molecular weight distribution of AAP extracted were studied. Two factors, ultrasonic wave and extraction time in water were screened from six factors . The singal-order tests and integrated curvature detection of the two factors were carried out. After that, the experiment domain approached to the optimum point, the optimum technology conditions of ultrasonic wave extraction of AAP were determined by central composite design: ultrasonic wave power 908W, extraction time 100°C, and the AAP yield of ultrasonic wave extraction approached to 24%. It was indicated that ultrasonic wave can promote the yield of the large molecular weight components by the analysis of molecular weight distribution.

scholarly journals Impact of Power Ultrasound on Antihypertensive Activity, Functional Properties, and Thermal Stability of Rapeseed Protein Hydrolysates

2017 ◽  
Vol 2017 ◽  
pp. 1-11 ◽  
Author(s):  
Asif Wali ◽  
Haile Ma ◽  
Muhammad Shahnawaz ◽  
Khizar Hayat ◽  
Jian Xiaong ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Inhibitory Activity ◽  
Surface Hydrophobicity ◽  
Protein Hydrolysates ◽  
Ace Inhibitory Activity ◽  
Power Ultrasound ◽  
Inhibitory Activities ◽  
Rapeseed Protein Hydrolysates ◽  
Thermal Stability Of ◽  
Ace Inhibitory

The effects of power ultrasound pretreatments on the degree of hydrolysis (DH), angiotensin-I-converting enzyme (ACE) inhibitory activity, amino acid composition, surface hydrophobicity, protein solubility, and thermal stability of ACE inhibition of rapeseed protein hydrolysates were evaluated. Ultrasonic pretreatments before enzymolysis in terms of power and exposure time increased the DH and ACE inhibitory activities over the control (without sonication). In this study, maximum DH 22.07% and ACE inhibitory activity 72.13% were achieved at 600 W and 12 min pretreatment. Compared to the hydrolysates obtained without sonication, the amino acid profile of ultrasound pretreated hydrolysates showed significant changes particularly in the proline content and hydrophobic amino acids with an increased rate of 2.47% and 6.31%, respectively. Ultrasound pretreatment (600 watts, 12 min) improved functional properties of protein hydrolysates over control by enhancing surface hydrophobicity and solubility index with an increased rate of 130.76% and 34.22%. Moreover, the stability test showed that the ACE inhibitory activity remains stable against heat treatments. However, extensive heat, prolonged heating time, and alkaline conditions were not in the favor of stability test, while under mild heat and acidic conditions their ACE inhibitory activities were not significantly different from unheated samples.

scholarly journals Chemical Characteristics and Activity of ACE Inhibitors on Fractionation of Tempeh Koro kratok (Phaseolus lunatus) Peptides

2020 ◽  
Vol 16 (2) ◽  
pp. 42
Author(s):  
Marta Tika Handayani ◽  
Retno Indrati ◽  
Muhammad Nur Cahyanto
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Inhibitory Activity ◽  
Chemical Properties ◽  
Ace Inhibition ◽  
Fermented Food ◽  
Phaseolus Lunatus ◽  
Ace Inhibitory Activity ◽  
Hydrophobic Amino Acid ◽  
Ace Inhibitory

Tempeh is a fermented food that is good for health and has high nutritional value. Koro kratok tempeh is one of tempeh which is made from non-soybean legumes. The fermentation process will convert macromolecular compounds to micromolecules thereby increasing bioavailability and providing functional properties. This study aimed to find out the chemical properties of koro kratok tempeh and the effect of peptide molecular weight of koro kratok tempeh on ACE inhibition activity. The results show that koro kratok seeds contained 20.66% protein which total hydrophobic amino acid was 3.32% (w/w protein). This hydrophobic amino acid was higher than that soybean, indicated that koro kratok (Phaseolus lunatus) has a potential producing ACE peptide inhibitors. The koro kratok seeds had ACE inhibitory activity  19.72%. This activity increased to 84.97% when the seeds were fermented for 48h to become tempeh. Peptide fractionation showed that the smaller the molecular weight of the peptide, the higher the ACE inhibitory activity.

scholarly journals Antihypertensive Effects of Virgin Olive Oil (Unfiltered) Low Molecular Weight Peptides with ACE Inhibitory Activity in Spontaneously Hypertensive Rats

Nutrients ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 271 ◽  
Author(s):  
Juan María Alcaide-Hidalgo ◽  
Miguel Romero ◽  
Juan Duarte ◽  
Eduardo López-Huertas
Keyword(s):  
Molecular Weight ◽  
Inhibitory Activity ◽  
Spontaneously Hypertensive Rats ◽  
Virgin Olive Oil ◽  
Antihypertensive Activity ◽  
Low Molecular Weight ◽  
Hypertensive Rats ◽  
Ace Inhibitory Activity ◽  
Spontaneously Hypertensive ◽  
Ace Inhibitory

The low molecular weight peptide composition of virgin olive oil (VOO) is mostly unknown. We hypothesised that unfiltered VOO could possess low molecular weight peptides with antihypertensive activity. We produced unfiltered VOO and obtained a water-soluble peptide extract from it. The peptides were separated by size-exclusion using fast protein liquid chromatography, and the low molecular weight fraction was analysed by nanoscale liquid chromatography-Orbitrap coupled with tandem mass spectrometry and de novo sequencing. We selected 23 peptide sequences containing between 6 and 9 amino acids and molecular masses ranging 698–1017 Da. Those peptides were chemically synthesised and their angiotensin-converting enzyme (ACE) inhibitory activity was studied in vitro. Seven peptides showed a strong activity, with half maximal inhibitory concentration (IC50) <10 µm. The antihypertensive effects of the four most active synthesised ACE inhibitor peptides were studied in spontaneously hypertensive rats (SHR). Acute oral administration of synthetic peptides RDGGYCC and CCGNAVPQ showed antihypertensive activity in SHR. We conclude that unfiltered VOO naturally contains low molecular weight peptides with specific ACE inhibitory activity and antihypertensive effects in SHR.

Angiotensin-I Converting Enzyme Inhibitory Peptides from Sweet Sorghum Grain Protein: Optimisation of Hydrolysis Conditions and Hydrolysate Characterization

2019 ◽  
Vol 41 (1) ◽  
pp. 175-175
Author(s):  
Jun Qiang Jia Jun Qiang Jia ◽  
Nan Miao Nan Miao ◽  
Jin Juan Du and Qiong Ying Wu Jin Juan Du and Qiong Ying Wu
Keyword(s):  
Inhibitory Activity ◽  
Sweet Sorghum ◽  
Grain Protein ◽  
Ace Inhibitory Activity ◽  
Molecular Weights ◽  
Competitive Inhibitors ◽  
Hydrolysis Temperature ◽  
Hydrolysis Conditions ◽  
Sorghum Grain ◽  
Ace Inhibitory

In order to utilize sweet sorghum grain protein (SSGP) for food applications, SSGP was hydrolyzed by alcalase to produce the hydrolysates with ACE-inhibitory activity. The Plackett-Burman design (PBD) was used to identify the important factors influencing the ACE-inhibitory activity of SSGP hydrolysates. The result of PBD indicated that hydrolysis temperature, pH and alcalase dosage had significant influence (P andlt; 0.05) on the ACE-inhibitory activity of SSGP hydrolysates. Response surface methodology (RSM) was applied to optimize the three significant factors. The optimum hydrolysis conditions obtained from RSM were as follows: hydrolysis temperature 56 and#176;C, pH 8.0, alcalase dosage 5200U/g. Under the optimum conditions, SSGP hydrolysates contained 24.3% 1–5 kDa (IC50=0.305 mg/ml) and 15.2% andlt;1 kDa (IC50=0.116 mg/ml) peptide fractions having potent in vitro ACE inhibitory activities. Moreover, the inhibition pattern against ACE investigated using Lineweaver–Burk plots revealed that the peptides with molecular weights above 5 kDa in the SSGP hydrolysates were non-competitive inhibitors with inhibition constants (Ki) between 1.098 and 1.171 mg/ml, while the peptides with molecular weights below 5 kDa in the hydrolysates were competitive inhibitors with Ki between 0.110 and 0.184 mg/ml. The results of this study suggest that SSGP may be considered as a source of functional ingredients for the prevention of hypertension.

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