scholarly journals Relationship between antioxidative potential and amino acids composition of the bioactive peptides prepared from Indian squid Uroteuthis (Photololigo) duvaucelii (d’Orbigny, 1835) using alcalase

2017 ◽  
Vol 64 ◽  
Author(s):  
Fathiraja Parthiban ◽  
Robinson Jeya Shakila ◽  
Geevaretnam Jeyasekaran ◽  
Rajendran Shalini
Keyword(s):  
Amino Acids ◽  
Functional Foods ◽  
Antioxidant Properties ◽  
Molecular Size ◽  
Protein Hydrolysates ◽  
Degree Of Hydrolysis ◽  
Amino Acids Composition ◽  
Amino Acid Profiles ◽  
Hydrophobic Amino Acids ◽  
Free Radicals Scavenging

Biopeptides derived from fish protein hydrolysates are gaining popularity as active ingredients in functional foods. In this study, squid protein hydrolysates (SPH) prepared from Uroteuthis (Photololigo) duvaucelii, using alcalase and their biopeptides fractionated using ultrafiltration were investigated for their antioxidant properties in relation to the changes intheir amino acid profiles. Squid mantle hydrolysed within 30 min with a degree of hydrolysis (DH) of 13.7%. SPH had 89% 2, 2-diphenyl-1- picrylhydrazyl (DPPH) inhibition, 94% 2, 2-azino-bis-(3-ethylbenzothiazoline-6-sulphonicacid) (ABTS) inhibition and 96% hydroxyl inhibition at 10 mg ml-1 concentration. In the squid peptides, DPPH inhibition increased with the decrease in the molecular size of peptides from 51% to 95% (3 Ka), ABTS radical inhibition was <42% for peptideswith >5KDa size and >95% for peptides with <5KDa. Hydroxyl radical inhibition increased from 75-98% with decrease in molecular size. Increase in glycine, alanine, leucine and taurine was noticed in peptides with MW <5KDa along with a decrease in methionine and arginine. Histidine, asparagine and tyrosine had also contributed to the activities of peptides with MW 3-5 KDa sizes. This study indicated that peptides with MW <5KDa had more free radicals scavenging activities with more hydrophobic amino acids, tyrosine and taurine which are mainly responsible for antioxidative properties. Therefore, squid peptides with MW <5KDa prepared using alcalase have potential to serve as nutraceuticals.

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.

Antioxidant Properties of Microalgae Protein Hydrolysates Prepared by Neutral Protease Digestion

2014 ◽  
Vol 707 ◽  
pp. 149-153 ◽  
Author(s):  
Xiao Hu ◽  
Xian Qing Yang ◽  
Lai Hao Li ◽  
Yan Yan Wu ◽  
Wan Ling Lin ◽  
...  
Keyword(s):  
Antioxidant Activities ◽  
Radical Scavenging Activity ◽  
Antioxidant Properties ◽  
Radical Scavenging ◽  
Reducing Power ◽  
Protein Hydrolysates ◽  
Neutral Protease ◽  
Degree Of Hydrolysis ◽  
Protease Digestion ◽  
Hydrolysis Of

Microalgae protein hydrolysates (MPH) were obtained by enzymatic hydrolysis of defatted microalgae meal using neutral protease. The protein recovery, degree of hydrolysis, and the antioxidant activities of the hydrolysates were investigated. The results demonstrated that hydrolysates prepared by neutral protease at 50 °C for 4 h exhibited the strongest antioxidant activity. Under these conditions, the 1,1-diphenyl-2-picrylhydrazyl (DPPH), hydroxyl radical scavenging activity and the reducing power of the hydrolysates were 68.3%, 50.8% and 1.303, respectively.

scholarly journals The Effect of Fermentation with Kefir Grains on the Physicochemical and Antioxidant Properties of Beverages from Blue Lupin (Lupinus angustifolius L.) Seeds

Molecules ◽  
2020 ◽  
Vol 25 (24) ◽  
pp. 5791
Author(s):  
Łukasz Łopusiewicz ◽  
Emilia Drozłowska ◽  
Paulina Trocer ◽  
Paweł Kwiatkowski ◽  
Artur Bartkowiak ◽  
...  
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Microbial Population ◽  
Antioxidant Properties ◽  
Lupinus Angustifolius ◽  
Kefir Grains ◽  
Antioxidant Properties Of Beverages ◽  
Hydrolysis Of ◽  
Free Radicals Scavenging

Plant derived fermented beverages have recently gained consumers’ interest, particularly due to their intrinsic functional properties and presence of beneficial microorganisms. Three variants containing 5%, 10%, and 15% (w/w) of sweet blue lupin (Lupinus angustifolius L. cv. “Boregine”) seeds were inoculated with kefir grains and incubated at 25 °C for 24 h. After processing, beverages were stored in refrigerated conditions (6 °C) for 21 days. Changes in microbial population, pH, bioactive compounds (polyphenolics, flavonoids, ascorbic acid), reducing sugars, and free amino acids were estimated. Additionally, viscosity, firmness, color, and free radicals scavenging properties were determined. Results showed that lactic acid bacteria as well as yeast were capable of growing well in the lupin matrix without any supplementation. During the process of refrigeration, the viability of the microorganisms was over the recommended minimum level for kefir products. Hydrolysis of polysaccharides as well as increase of free amino acids was observed. As a result of fermentation, the beverages showed excellent DPPH, ABTS+·, ·OH, and O2− radicals scavenging activities with a potential when considering diseases associated with oxidative stress. This beverages could be used as a new, non-dairy vehicle for beneficial microflora consumption, especially by vegans and lactose-intolerant consumers.

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 Properties of Peanut (KAC431) Protein Hydrolysates and Their Impact on the Quality of Gluten-Free Rice Bread

Foods ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. 942 ◽  
Author(s):  
Suphat Phongthai ◽  
Nuttapon Singsaeng ◽  
Rossarin Nhoo-ied ◽  
Thipubol Suwannatrai ◽  
Regine Schönlechner ◽  
...  
Keyword(s):  
Amino Acids ◽  
Functional Properties ◽  
Positive Impact ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Hydrolysates ◽  
Degree Of Hydrolysis ◽  
Major Protein ◽  
Gluten Free ◽  
Major Protein Band

Protein hydrolysates (PH) with a degree of hydrolysis (DH) of 5%, 10%, and 13% from two varieties of peanut were prepared using two commercial enzymes, Alcalase and Flavourzyme. The content of essential amino acids (30,290 mg/100 g) and hydrophobic amino acids (34,067 mg/100 g) of the peanut variety Kalasin 2 (KAC431) protein was higher than that of a common variety, Kalasin 1 (KAC1) (p < 0.05). The protein molecular weight distributions of the two varieties of peanut detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) were similar, ranging from 15 to 75 kDa, with a major protein band at 50–75 kDa. The antioxidant and functional properties of derived PHs were influenced by DH. Although the foaming ability of protein was improved by DH5%, it was obviously decreased upon increasing DH further. The best emulsifying properties were observed in PH with DH5% (p < 0.05). The incorporation of PH with a small DH, especially when produced using Flavourzyme, had a highly positive impact on the specific volume and relative elasticity of gluten-free bread. The effect of PHs on bread quality was highly correlated with their functional properties. This study suggests that partially enzymatically modified proteins are suitable for incorporation in food products such as bread and other gluten-free products.

Antioxidant Properties of Tilapia Component Protein Hydrolysates and the Membrane Ultrafiltration Fractions

2014 ◽  
Vol 1073-1076 ◽  
pp. 1812-1817 ◽  
Author(s):  
Xing Xing Chen ◽  
Xiao Hu ◽  
Lai Hao Li ◽  
Xian Qing Yang ◽  
Yan Yan Wu ◽  
...  
Keyword(s):  
Antioxidant Activities ◽  
Protein Hydrolysate ◽  
Antioxidant Properties ◽  
Radical Scavenging ◽  
Reducing Power ◽  
Molecular Size ◽  
Myofibrillar Protein ◽  
Degree Of Hydrolysis ◽  
Sarcoplasmic Protein ◽  
Radical Scavenging Ability

In this study, three kinds of component proteins of tilapia were hydrolyzed with papain for 4h. The effect of hydrolysis and the antioxidant activities of the resulting hydrolysates were characterized. The results showed sarcoplasmic protein hydrolysate had significantly (p < 0.05) highest scavenging ability against hydroxyl, superoxide, DPPH radicals and the total reducing power. Stroma protein hydrolysate had the highest nitrogen recovery (NR) while myofibrillar protein hydrolysate had the highest degree of hydrolysis (DH). Sarcoplasmic protein hydrolysate with high radical scavenging ability was separated by membrane ultrafiltration into four molecular size fractions (<5, 5–10, 10–100, >100kDa). It was found that the antioxidant activities of the <5kDa fraction were higher than that of other fractions. Overall, sarcoplasmic protein is more efficient to obtain antioxidant properties when compared to other component proteins of tilapia.

scholarly journals Amino Acid Profiles of the Flesh of the Heterosexual Pairs of Neopetrolisthes maculatus

2017 ◽  
Vol 61 ◽  
pp. 23-35 ◽  
Author(s):  
Emmanuel Ilesanmi Adeyeye
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Essential Amino Acid ◽  
Essential Amino Acids ◽  
Efficiency Ratio ◽  
Amino Acids Composition ◽  
Amino Acid Requirements ◽  
Amino Acid Profiles ◽  
Limiting Amino Acid ◽  
Acid Index

This paper reports on amino acid profiles of the flesh of heterosexuals of porcellanids collected from the Atlantic Ocean at Orimedu beach in Ibeju-Lekki, Lagos, Nigeria. Results showed that high values of amino acids were observed in the heterosexual flesh of Neopetrolisthes maculatus (g 100g-1 protein): 17.7 – 17.8 (Glu), 9.90 – 10.0 (Asp), 8.70 – 9.07 (Arg), 7.23 – 7.94 (Leu) and 5.81 – 6.06 (Gly). Total essential amino acid values ranged from 45.2 – 46.2 g 100-1g. Predicted protein efficiency ratio was 3.82 – 4.14, the range of essential amino acid index was 86.9 – 89.9, the biological values ranged from 83.0 – 86.3. The Lys/Trp was 3.31-4.27. Serine was limiting amino acid (0.513 – 0.516) in the egg score comparison; under the essential amino acids scores, Lys (0.840) was limiting in female but Val (0.823) was limiting in the male; Lys (0.796 – 0.905) was limiting in both samples in the pre-school child amino acid requirements. It was observed that out of the twenty parameters determined, male flesh was more concentrated in 60% values than the female flesh and 40% better in female than male. Correlation coefficient result showed that significant differences existed in the amino acids composition at r = 0.01 of the N. maculatus samples.

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.

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