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

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.

scholarly journals INHIBITING ACTIVITY OF ANGIOTENSIN CONVERTING ENZYME-1 BY BEAN PROTEIN HYDROLYSATE GENUS PHASEOLUS

2021 ◽  
Vol 18 (2) ◽  
pp. 75
Author(s):  
Tejasari Tejasari ◽  
Faiqotul Aulia ◽  
Nurdiana Agustina
Keyword(s):  
Amino Acids ◽  
G Protein ◽  
Protein Hydrolysate ◽  
Lima Bean ◽  
Protein Hydrolysates ◽  
Kidney Bean ◽  
Phaseolus Lunatus ◽  
Hydrophobic Amino Acids ◽  
Hydrolysis Of ◽  
Bean Protein

Kidney bean (Phaseolus.vulgaris L. Chitra) and lima bean (Phaseolus lunatus L. Sweet) hydrolysates were obtained by alcalase and flavourzyme hydrolysis of the bean seed protein. Peptide in the bean hydrolysates, with hydrophobic amino acids had been studied for their inhibitory ACE-1 activity preventing transformation into ACE-2 that prevention hypertension. This study aimed to measure inhibitory ACE-1 activity of protein hydrolyzates from the bean Phaseolus genus spp. grown in Jember, and its solubility. The bean protein (19.8-20,2%) was extracted using isoelectric precipitation at pH 4-4,6. The extract were hydrolyzed at pH 8-9 for alcalase and pH 7 for flavourzyme, followed with inactivation at 80-85 o C. ACE-1 inhibitory activity was measured based on the amount of hippuric acid (HA) formed by the hydrolysis of Hippuryl-His-Leu (HHL) in spectrophotometry detection method (228 nm). The ultra chromatography evaluation showed that the protein hydrolysates of kidney bean contained higher hydrophobic amino acids (455.5 mg/g protein) compare to those of lima bean (350 mg/g protein). Protein hydrolysates of both beans from alcalase hydrolysis have higher ACE-1 inhibitory rather than those from flavourzyme. Protein hydrolysate from Phaseolus spp bean protein hydrolysis by alcalase, contain small molecular weight peptides (3.9-22.6 kDa) high ACE-1 inhibition ability (83 -88%), and therefore suggested as antihypertensive nutraceuticals. Highest solubility of protein hydrolysate resulted from alcalase hydrolysis of both beans were observed at pH 8-9, while those resulted from flavorzyme hydrolysis were at pH 7.

scholarly journals Kinetics of Hyaluronidase Inhibition by Rice (Oryza sativa L.) Protein Hydrolysate

2020 ◽  
Vol 10 (24) ◽  
pp. 9087
Author(s):  
Hui-Ju Chen ◽  
Fan-Jhen Dai ◽  
Siao-Ling Fan ◽  
Yu-Chun Huang ◽  
Chi-Fai Chau ◽  
...  
Keyword(s):  
Amino Acids ◽  
Inhibitory Activity ◽  
Protein Hydrolysate ◽  
Oryza Sativa L ◽  
Skin Aging ◽  
Protein Hydrolysates ◽  
Total Amino Acid ◽  
Competitive Reaction ◽  
Rice Protein

Research on the skin’s maintenance and protection against aging has gradually progressed toward phytocosmetics. This study investigated the in vitro hyaluronidase inhibitory activity of rice protein hydrolysate obtained by using bacterial amylase and protease against skin aging-related enzymes. Here, the molecular weights of rice protein hydrolysates were in the range 5–63 kDa. Every 100 g of a rice protein hydrolysate contains approximately 2960 mg of total amino acid, including essential amino acids (893 mg) and branched-chain amino acids (591 mg). A kinetic study showed that hyaluronidase inhibition by the rice protein hydrolysate occurs through a competitive reaction mechanism. Achieving effective hyaluronidase inhibitory activity, the rice protein hydrolysate had a half maximal inhibitory concentration of 7.61 mg/mL. Because hyaluronidase activity inhibition is crucial for treating skin aging, rice protein hydrolysates should be considered as cosmeceutical ingredients.

Comparison of Yield, Antioxidant Activity and Functional Properties of Protein Hydrolysates from Tuna and Pollock Frame

2012 ◽  
Vol 554-556 ◽  
pp. 1327-1331
Author(s):  
Li Jun Zhang ◽  
Qian Cheng Zhao ◽  
Bing Bing Wang ◽  
Xue Wan ◽  
Zhi Bo Li ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Functional Properties ◽  
Protein Hydrolysate ◽  
Protein Hydrolysates ◽  
Degree Of Hydrolysis ◽  
Basic Composition ◽  
Foaming Ability ◽  
Hydrolysis Of ◽  
Better Than

Protein hydrolysates from Tuna frame (TFPH) and Pollock frame (PFPH) were prepared by papain, respectively.The yield, the basic composition content, the antioxidant activity and functional properties (solubility, emulsifying and foaming ability) and the degree of hydrolysis of the protein hydrolysates were evaluated. Results suggest that solubility, antioxidant activity of protein hydrolysate from Pollock frame are better than that of tuna frame, but the yield is lower than that of tuna frame.

scholarly journals Sport Nutrition Drinks Based on Octopus Protein Hydrolysate

2016 ◽  
Vol 19 (3) ◽  
pp. 339 ◽  
Author(s):  
Bambang Riyanto ◽  
Wini Trilaksani ◽  
Rika Lestari
Keyword(s):  
Amino Acids ◽  
Protein Hydrolysate ◽  
Soybean Protein ◽  
Protein Hydrolysates ◽  
Sport Nutrition ◽  
Degree Of Hydrolysis ◽  
Protein Hydrolyzate ◽  
Whey Protein Hydrolysates ◽  
Marine Product ◽  
Serving Size

Sport nutrition drinks are well-known in escalating athlete’s performance and endurance. These product developed from whey protein hydrolysates and soybean protein hydrolysates have already been recognized, however expansion from marine product is comparatively rare. Octopus (Octopus cyanea) widely acknowledged containing taurine and rich in amino acids is potential to be developed as ingredient for sport nutrition drink. The aims of this study were to create and characterize sport nutrition drinks based on marine peptides through Octopus protein hydrolyzate. Octopus protein hydrolysate has 77.78 ± 2.69% degree of hydrolysis and 751.02 ± 10.63 mg / 100g taurine. Sports nutrition drinks with the addition of 4% Octopus protein hydrolyzate was acceptable sensory panelists, and the serving size of 600 ml contained taurine 726.06 ± 0.82 mg and detected 17 types of amino acids.

scholarly journals Modeling the QSAR of ACE-Inhibitory Peptides with ANN and Its Applied Illustration

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Ronghai He ◽  
Haile Ma ◽  
Weirui Zhao ◽  
Wenjuan Qu ◽  
Jiewen Zhao ◽  
...  
Keyword(s):  
Amino Acids ◽  
Inhibitory Activity ◽  
Structural Information ◽  
Qsar Model ◽  
Ace Inhibitory Activity ◽  
Activity Data ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Hydrophobic Amino Acids ◽  
Ace Inhibitory

A quantitative structure-activity relationship (QSAR) model of angiotensin-converting enzyme- (ACE-) inhibitory peptides was built with an artificial neural network (ANN) approach based on structural or activity data of 58 dipeptides (including peptide activity, hydrophilic amino acids content, three-dimensional shape, size, and electrical parameters), the overall correlation coefficient of the predicted versus actual data points is , and the model was applied in ACE-inhibitory peptides preparation from defatted wheat germ protein (DWGP). According to the QSAR model, the C-terminal of the peptide was found to have principal importance on ACE-inhibitory activity, that is, if the C-terminal is hydrophobic amino acid, the peptide's ACE-inhibitory activity will be high, and proteins which contain abundant hydrophobic amino acids are suitable to produce ACE-inhibitory peptides. According to the model, DWGP is a good protein material to produce ACE-inhibitory peptides because it contains 42.84% of hydrophobic amino acids, and structural information analysis from the QSAR model showed that proteases of Alcalase and Neutrase were suitable candidates for ACE-inhibitory peptides preparation from DWGP. Considering higher DH and similar ACE-inhibitory activity of hydrolysate compared with Neutrase, Alcalase was finally selected through experimental study.

BIOCHEMICAL ASPECTS OF INTRAVENOUS ALIMENTATION

PEDIATRICS ◽  
1971 ◽  
Vol 48 (6) ◽  
pp. 955-965
Author(s):  
H. Ghadimi ◽  
F. Abaci ◽  
S. Kumar ◽  
M. Rathi
Keyword(s):  
Amino Acids ◽  
Protein Hydrolysate ◽  
Newborn Infants ◽  
Liver Function Tests ◽  
Protein Hydrolysates ◽  
High Concentration ◽  
Parenteral Alimentation ◽  
Intravenous Alimentation ◽  
Very High

Biochemical aspects of total parenteral alimentation in 10 patients (two low birth weight newborn infants and eight infants) for periods of 5 to 24 days were studied by: A. Determination of concentration of amino acids and ammonia of two commercially available protein hydrolysates. B. Analyses of blood and urine obtained before, during, and after parenteral alimentation for various biochemical parameters including amino acids, urea nitrogen, glucose, and osmolality. The results showed that the protein hydrolysates contained a very high concentration of ammonia. This inordinate amount of ammonia taxes the Krebs urea cycle and in premature infants enhances acidosis and respiratory distress syndrome. It also explains the abnormal liver function tests and hyperammonemia found concomitantly with infusion of protein hydrolysate. Another effect of infusion of protein hydrolysate, in conventional amount, is persistent hyperaminoacidemia.

The hydrophobic amino acids in putative helix 8 in carboxy-terminus of histamine H3 receptor are involved in receptor-G-protein coupling

2011 ◽  
Vol 23 (11) ◽  
pp. 1843-1849 ◽  
Author(s):  
Atsuo Kuramasu ◽  
Jun Sukegawa ◽  
Takeya Sato ◽  
Eiko Sakurai ◽  
Takehiko Watanabe ◽  
...  
Keyword(s):  
Amino Acids ◽  
G Protein ◽  
Carboxy Terminus ◽  
G Protein Coupling ◽  
Histamine H3 Receptor ◽  
Protein Coupling ◽  
H3 Receptor ◽  
Hydrophobic Amino Acids ◽  
Histamine H3

Mung-bean Protein Hydrolysates Obtained with Alcalase Exhibit Angiotensin I-converting Enzyme Inhibitory Activity

2005 ◽  
Vol 11 (4) ◽  
pp. 281-287 ◽  
Author(s):  
Guan Hong Li ◽  
Guo Wei Le ◽  
Huan Liu ◽  
Yong Hui Shi
Keyword(s):  
Inhibitory Activity ◽  
Mung Bean ◽  
Protein Hydrolysates ◽  
Antihypertensive Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory ◽  
Bean Protein

Mung-bean protein isolates were hydrolysed by two proteases alcalase and neutrase commercially available for food industry use, and the angiotensin I-converting enzyme (ACE) inhibitory activities of the enzymatic hydrolysates were measured at different hydrolysis times. The non-hydrolysed protein showed no inhibitory activity. Hydrolysates generated with neutrase displayed very low ACE inhibitory activity, while those obtained with alcalase exhibited high inhibitory activity. The highest ACE inhibitory activity with the IC50 value of 0.64 mg protein/mL was found in the hydrolysate obtained with alcalase at 2h of hydrolysis time. These results indicated that mung-bean protein is a good protein source of ACE inhibitory peptides when hydrolysed with the protease alcalase. The mung-bean protein hydrolysates prepared with alcalase might be utilised for physiologically functional foods with antihypertensive activity.

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