scholarly journals Sport Nutrition Drinks Based on Octopus Protein Hydrolysate

2017 ◽  
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

<p>Abstract<br />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.</p>

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 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 Soluble Whey Protein Hydrolysate Ameliorates Muscle Atrophy Induced by Immobilization via Regulating the PI3K/Akt Pathway in C57BL/6 Mice

Nutrients ◽  
2020 ◽  
Vol 12 (11) ◽  
pp. 3362
Author(s):  
Ji Eun Shin ◽  
Seok Jun Park ◽  
Seung Il Ahn ◽  
Se-Young Choung
Keyword(s):  
Skeletal Muscle ◽  
Whey Protein ◽  
Muscle Mass ◽  
Muscle Atrophy ◽  
Skeletal Muscle Mass ◽  
Protein Hydrolysate ◽  
Protein Hydrolysates ◽  
Protein Supplementation ◽  
Whey Protein Hydrolysates ◽  
Whey Protein Hydrolysate

Sarcopenia, a loss of skeletal muscle mass and function, is prevalent in older people and associated with functional decline and mortality. Protein supplementation is necessary to maintain skeletal muscle mass and whey protein hydrolysates have the best nutrient quality among food proteins. In the first study, C57BL/6 mice were subjected to immobilization for 1 week to induce muscle atrophy. Then, mice were administered with four different whey protein hydrolysates for 2 weeks with continuous immobilization. Among them, soluble whey protein hydrolysate (WP-S) had the greatest increase in grip strength, muscle weight, and cross-sectional area of muscle fiber than other whey protein hydrolysates. To investigate the molecular mechanism, we conducted another experiment with the same experimental design. WP-S significantly promoted the phosphoinositide 3-kinase (PI3K)/protein kinase B (Akt)/mammalian target of rapamycin (mTOR) pathway and inhibited the PI3K/Akt/forkhead box O (FoxO) pathway. In addition, it increased myosin heavy chain (MyHC) expression in both the soleus and quadriceps and changed MyHC isoform expressions. In conclusion, WP-S attenuated muscle atrophy induced by immobilization by enhancing the net protein content regulating muscle protein synthesis and degradation. Thus, it is a necessary and probable candidate for developing functional food to prevent sarcopenia.

scholarly journals Debittering of Protein Hydrolysates by Lactobacillus LBL-4 Aminopeptidase

2011 ◽  
Vol 2011 ◽  
pp. 1-7 ◽  
Author(s):  
Bozhidar Tchorbanov ◽  
Margarita Marinova ◽  
Lydia Grozeva
Keyword(s):  
Culture Media ◽  
Protein Hydrolysate ◽  
Protein Hydrolysates ◽  
Cell Protein ◽  
Degree Of Hydrolysis ◽  
Gel Chromatography ◽  
Cell Free Extract ◽  
Food Grade ◽  
Enzyme Action

Yoghurt strain Lactobacillus LBL-4 cultivated for 8–10 h at pH ~6.0 was investigated as a considerable food-grade source of intracellular aminopeptidase. Cell-free extract manifesting >200 AP U/l was obtained from cells harvested from 1 L culture media. Subtilisin-induced hydrolysates of casein, soybean isolate, and Scenedesmus cell protein with degree of hydrolysis 20–22% incubated at 45∘C for 10 h by 10 AP U/g peptides caused an enlarging of DH up to 40–42%, 46–48%, and 38–40% respectively. The DH increased rapidly during the first 4 h, but gel chromatography studies on BioGel P-2 showed significant changes occurred during 4–10 h of enzyme action when the DH increased gradually. After the digestion, the remained AP activity can be recovered by ultrafiltration (yield 40–50%). Scenedesmus protein hydrolysate with DH 20% was inoculated by Lactobacillus LBL-4 cells, and after 72 h cultivation the DH reached 32%. The protein hydrolysates (DH above 40%) obtained from casein and soybean isolate (high Q value) demonstrated a negligible bitterness while Scenedesmus protein hydrolysates (low Q value) after both treatments were free of bitterness.

scholarly journals Degree of Hydrolysis Affects the Techno-Functional Properties of Lesser Mealworm Protein Hydrolysates

Foods ◽  
2020 ◽  
Vol 9 (4) ◽  
pp. 381 ◽  
Author(s):  
Giulia Leni ◽  
Lise Soetemans ◽  
Augusta Caligiani ◽  
Stefano Sforza ◽  
Leen Bastiaens
Keyword(s):  
Enzymatic Hydrolysis ◽  
Functional Properties ◽  
Protein Hydrolysate ◽  
Preliminary Test ◽  
Protein Hydrolysates ◽  
Degree Of Hydrolysis ◽  
Potential Implication ◽  
Alphitobius Diaperinus ◽  
Positive Effects ◽  
Lesser Mealworm

Protein hydrolysates from lesser mealworm (Alphitobius diaperinus, LM) were obtained by enzymatic hydrolysis with protease from Bacillus licheniformis. A preliminary test performed for five hours of hydrolysis generated an insect protein hydrolysate with 15% of degree of hydrolysis (DH), optimum solubility property and oil holding capacity, but emulsifying and foaming ability were completely impaired. In order to investigate the potential implication of DH on techno-functional properties, a set of protein hydrolysates with a different DH was obtained by sub-sampling at different time points during three hours of enzymatic hydrolysis process. An increase in DH% had positive effects on the solubility property and oil holding ability, while a reduced emulsifying ability was observed up to five hours of hydrolysis. These results demonstrated that the enzymatic hydrolysis, if performed under controlled conditions and not for a long period, represents a valid method to extract high quality protein from insects with tailored techno-functionality, in order to produce tailored ingredients for feed and food purpose.

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 Physicochemical and sensory characteristics of whey protein hydrolysates generated at different total solids levels

2004 ◽  
Vol 72 (2) ◽  
pp. 138-143 ◽  
Author(s):  
David Spellman ◽  
Gerard O'Cuinn ◽  
Richard J FitzGerald
Keyword(s):  
Whey Protein ◽  
Whey Proteins ◽  
Reversed Phase ◽  
Protein Hydrolysates ◽  
Degree Of Hydrolysis ◽  
Total Solids ◽  
Whey Protein Hydrolysates ◽  
Peptide Peak ◽  
Hydrophobic Peptide ◽  
Physical And Chemical

Whey protein hydrolysates were generated at different total solids (TS) levels (50–300 g/l) using the commercially available proteolytic preparation Debitrase™ HYW20, while enzyme to substrate ratio, pH and temperature were maintained constant. Hydrolysis proceeded at a faster rate at lower TS reaching a degree of hydrolysis (DH) of 16·6% at 300 g TS/l, compared with a DH of 22·7% at 50 g TS/l after 6 h hydrolysis. The slower breakdown of intact whey proteins at high TS was quantified by gel-permeation HPLC. Reversed-phase (RP) HPLC of hydrolysate samples of equivalent DH (~15%) generated at different TS levels indicated that certain hydrophobic peptide peaks were present at higher levels in hydrolysates generated at low TS. Sensory evaluation showed that hydrolysates with equivalent DH values were significantly (P<0·0005) less bitter when generated at 300 g TS/l (mean bitterness score=25·4%) than hydrolysates generated at 50 g TS/l (mean bitterness score=39·9%). A specific hydrophobic peptide peak present at higher concentrations in hydrolysates generated at low TS was isolated and identified as β-lactoglobulin f(43–57), a fragment having the physical and chemical characteristics of a bitter peptide.

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.

Study on Hydrolysis Conditions of Flavourzyme in Soybean Polypeptide Alcalase Hydrolysate

2013 ◽  
Vol 652-654 ◽  
pp. 435-438 ◽  
Author(s):  
Yong Sheng Ma ◽  
Lin Tong Wang ◽  
Xian Hui Sun ◽  
Bing Chen Ma ◽  
Jian Wen Zhang ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Weight Distribution ◽  
Bitter Taste ◽  
Protein Hydrolysate ◽  
Soybean Protein ◽  
Hydrolysis Reaction ◽  
Protein Recovery ◽  
Degree Of Hydrolysis ◽  
Hydrolysis Conditions ◽  
Hydrolysis Of

Soybean protein Alcalase hydrolysate was further hydrolyzed by adopting Flavourzyme. From this further hydrolysis reaction, bitter of soybean polypeptide mixture was reduced distinctly. The optimal hydrolysis conditions of Flavourzyme was determined as that pH was 7.0 at temperature 50°C and E/S(ratio of enzyme and substrate) was 20LAPU/g. Bitter taste value was reduced to 2 after Flavourzyme hydrolysis reaction for 2 hours in optimal hydrolysis conditions. The change of molecular weight distribution range from Alcalase hydrolysate to Flavourzyme hydrolysate was not obvious. DH (Degree of hydrolysis) of soybean protein hydrolysate was increased to 24.2% which was improved 3.5% than Alcalase hydrolysate. Protein recovery proportion was increased to 73.2% which was improved 0.8% than Alcalase hydrolysate.

scholarly journals Aktivitas Antioksidan Hidrolisat Protein Ikan Cunang (Congresox talabon)

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Anggi Angelita Hermaya ◽  
Edison Edison ◽  
Andarini Diharmi
Keyword(s):  
Antioxidant Activity ◽  
Protein Content ◽  
Protein Hydrolysate ◽  
Enzyme Concentration ◽  
Enzyme Hydrolysis ◽  
Raw Material ◽  
Degree Of Hydrolysis ◽  
Protein Hydrolyzate ◽  
Fish Meat ◽  
Dpph Method

Cunang fish (Congresox talabon) has the potential as a raw material for fish protein hydrolyzates. Hydrolysis of cunang fish using the enzyme papain were produced peptides and amino acids that have antioxidant activity. The aim of this study was to determine the antioxidant activity of the protein hydrolyzate of cunang fish using different papain enzyme concentrations. This study used an experimental method with a completely randomized non-factorial design with three replications, with different papain enzyme concentrations (2%, 4%, 6%). The analysis parameters consisted of proximate content analysis in fish meat, degree of hydrolysis, the dissolved protein of the Bradford method, and the antioxidant activity of the DPPH method on the protein hydrolysate.  The results showed that the protein content of cunang fish had 73.15% (bk). The papain enzyme concentration of 6% was the best concentration hydrolyze cunang meat, is produced. protein hydrolysate.  The results of the protein hydrolyzate analysis showed that the degree of hydrolysis was 46.23%, the dissolved protein was 11.64% and the antioxidant activity was 549.16 ppm. Enzyme hydrolysis can increase dissolved protein content which is directly proportional to the increase in antioxidant activity.

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