scholarly journals Optimization of enzymatic hydrolysis of Pleurotus ostreatus derived proteins through RSM and evaluation of nutritional and functional qualities of mushroom protein hydrolysates

2022 ◽  
Vol 25 ◽  
Author(s):  
Bhaswati Goswami ◽  
Sayari Majumdar ◽  
Ruma Dutta ◽  
Jayati Bhowal
Keyword(s):  
Protein Content ◽  
Pleurotus Ostreatus ◽  
Protein Hydrolysate ◽  
Protein Hydrolysates ◽  
Proteinase K ◽  
Degree Of Hydrolysis ◽  
Different Temperatures ◽  
Assay Methods ◽  
Foaming Capacity ◽  
Hydrolysis Of

Abstract Pleurotus ostreatus (Jacq.) P. Kumm., the second most widely cultivated oyster mushroom was grown on paddy straw, which is cheap and readily available waste material. After harvesting and drying, nutritional, and antinutritional composition of P. ostreatus were estimated using the standard assay methods. Tannin and phytic acid were present in very negligible amount (0.095 ± 0.027 mg/g and 0.150 ± 0.083 mg/g, respectively), whereas oxalate and cyanide were absent in whole mushroom. In fact, P. ostreatus was hydrolysed with commercially available proteinase K, pepsin and trypsin with different concentrations of the enzymes (0.05%, 0.10% and 0.15%), at different temperatures (30 °C, 40 °C and 50 °C) for different time periods (60, 90 and 120 min) to get the mushroom protein hydrolysates. Degree of hydrolysis and protein content varied from 4.29 ± 1.12% to 99.42 ± 0.02% and from 0.25 ± 0.07 mg/mL to 3.22 ± 0.12 mg/mL, respectively. Maximum degree of hydrolysis and the highest protein content of protein hydrolysate was obtained when using 0.15% proteinase K, at 50 °C for 120 minutes. Mushroom protein hydrolysates thus obtained exhibited improved functional characteristics such as foaming capacity, foaming stability and emulsifying property than the unhydrolysed mushroom. Based on the result of the present study, the mushroom protein hydrolysates could be served as useful ingredient for food and nutraceutical applications.

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 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 Enzymatic hydrolysis of defatted soy flour by three different proteases and their effect on the functional properties of resulting protein hydrolysates

2011 ◽  
Vol 20 (No. 1) ◽  
pp. 7-14 ◽  
Author(s):  
M. Hrčková ◽  
M. Rusňáková ◽  
J. Zemanovič
Keyword(s):  
Enzymatic Hydrolysis ◽  
Functional Properties ◽  
Aqueous Dispersion ◽  
Protein Hydrolysates ◽  
Soy Flour ◽  
Degree Of Hydrolysis ◽  
Defatted Soy Flour ◽  
Sds Page ◽  
Soy Protein Hydrolysates ◽  
Hydrolysis Of

Commercial defatted soy flour (DSF) was dispersed in distilled water at pH 7 to prepare 5% aqueous dispersion. Soy protein hydrolysates (SPH) were obtained by enzymatic hydrolysis of the DSF using three different proteases (Flavourzyme 1000 L, No-vozym FM 2.0 L and Alcalase 2.4 L FG). The highest degree of hydrolysis (DH 39.5) was observed in the presence of protease Flavourzyme. SPH were used for measuring functional properties (foaming stability, gelation). Treatment with Flavourzyme improved foaming of proteins of DSF. Foaming stability was low in the presence of Novozym. Proteases treated DSF showed good gelation properties, mainly in the case of treatment with Flavourzyme. SDS-PAGE analysis showed that after enzyme ad-dition to the 5% aqueous dispersion of DSF each enzyme degraded both b-conglycinin and glycinin. In general, the basic polypeptide from glycinin showed the highest resistance to proteolytic activity. The most abundant free amino acids in the hydrolysates were histidine (30%), leucine (24%) and tyrosine (19%) in the case of the treatment with proteases Alcalase and Novozym, and arginine (22.1%), leucine (10.6%) and phenylalanine (12.9%) in the case of the treatment with Flavourzyme.  

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.

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 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.

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 Effect of pepsin hydrolysis on antioxidant activity of jellyfish protein hydrolysate

2021 ◽  
Vol 302 ◽  
pp. 02010
Author(s):  
Pratchaya Muangrod ◽  
Wiriya Charoenchokpanich ◽  
Vilai Rungsardthong ◽  
Savitri Vatanyoopaisarn ◽  
Benjamaporn Wonganu ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Protein Hydrolysate ◽  
Inhibitory Effect ◽  
Raw Material ◽  
Degree Of Hydrolysis ◽  
Dpph Radical ◽  
Radical Scavengers ◽  
Hydrolysis Time ◽  
Hydrolysis Of ◽  
By Products

Edible jellyfish have been consumed as food for more than a century with offering high protein and crunchy texture. The pepsin hydrolysis of jellyfish protein yields jellyfish protein hydrolysate (ep-JPH), reported for potential bioactivities such as antioxidant activity or antihypertensive activities. Due to the substantial number of by-products generated from jellyfish processing, the by-products were then selected as a raw material of JPH production. This research aimed to evaluate the effect of the hydrolysis time of pepsin on the antioxidant activity of ep-JPH. The dried desalted jellyfish by-products powder was enzymatically hydrolysed by 5% (w/w) pepsin, and the hydrolysis time was varied from 6, 12, 18, and 24 h at 37oC. Results showed that increased hydrolysis time increased the degree of hydrolysis (DH) and inhibition of DPPH radical. The 24 h ep-JPH possessed the highest DH and the highest inhibitory effect of DPPH radical. The results demonstrated that, in this experiment, all ep-JPHs were DPPH radical scavengers, exhibiting different inhibition activities depending on DH values.

Optimization of enzymatic protein hydrolysis conditions of Asiatic hard clam (Meretrix meretrix)

Food Research ◽  
2021 ◽  
Vol 5 (4) ◽  
pp. 153-162
Author(s):  
M.K. Zainol ◽  
F.W. Abdul Sukor ◽  
A. Fisal ◽  
T.C. Tuan Zainazor ◽  
M.R. Abdul Wahab ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Protein Hydrolysate ◽  
Hard Clam ◽  
Degree Of Hydrolysis ◽  
Protein Hydrolysis ◽  
Meretrix Meretrix ◽  
Optimum Conditions ◽  
Hydrolysis Time ◽  
Hydrolysis Conditions ◽  
Hydrolysis Of

This study was aimed to optimise the Alcalase® enzymatic hydrolysis extraction of Asiatic hard clam (AHC) (Meretrix meretrix) protein hydrolysate in terms of hydrolysis time, hydrolysis temperature, hydrolysis pH, and concentration of enzyme. Protein hydrolysate produced from AHC (M. meretrix) meat was used to determine the optimum hydrolysis conditions. Hydrolysis of AHC meat was optimised using the Central Composite Design Response Surface Methodology (RSM) (CCD). The relationship between four parameters such as temperature (45 – 65°C), enzyme to substrate concentration (1 – 2%), hydrolysis time (60 – 180 mins), and pH (7.5 – 9.5) to the degree of hydrolysis was investigated. The optimum conditions for enzymatic hydrolysis of AHC meat to achieve the maximum degree of hydrolysis (DH) were observed at 65°C, enzyme to substrate concentration of 1%, hydrolysis time of 60 mins, and pH 7.5. The enzymatic protein hydrolysis of AHC meat was predicted using a two factors interaction (2FI) model. Under these optimum conditions, DH's predicted value was 97.41%, which was close to the experimental value (97.89%). The freeze-dried protein hydrolysate powder was characterized concerning the proximate composition. Proximate analysis revealed that the AHC meat contains 7.92±1.76% of moisture, 2.23±0.89% of crude fat, 1.98±0.82 of ash, and 10.53±0.04% of crude protein. While the Asiatic hard clam protein hydrolysate (AHCPH) composed 9.12±0.02% of moisture, 0.80±0.29% of crude fat, and 27.76±0.10% of ash. The protein hydrolysate produced also contained high protein content (50.09±0.88%) and may serve as a good protein source.

scholarly journals Enzymatic Fractionation of Protein, Fat and Chitin from Hermetia illucens (L.) (Diptera: Stratiomyidae)

Proceedings ◽  
2020 ◽  
Vol 36 (1) ◽  
pp. 187
Author(s):  
Michael Josias Woods ◽  
Louwrens Christiaan Hoffman ◽  
Elsje Pieterse ◽  
Neill Jurgens Goosen
Keyword(s):  
Protein Hydrolysate ◽  
Protein Solubility ◽  
Amino Acid Profile ◽  
Process Conditions ◽  
Degree Of Hydrolysis ◽  
Hermetia Illucens ◽  
Hydrolysis Conditions ◽  
Hydrolysis Of ◽  
Central Composite ◽  
By Products

Abstract: Insects have the ability to convert biowaste into valuable functional compounds, such as proteins, fat and chitin. Currently, unlike with conventional commodities, there are few fractionation methods to isolate these compounds for diversification of use. Enzymatic hydrolysis is a possible method to fractionate Hermetia illucens larvae, into protein, fat and chitin. This method is a particularly attractive due to the milder process conditions required compared to chemical methods, the relative ease to control the reaction and minimal formation of unpalatable and toxic by-products. A central composite design was used to help identify the optimum hydrolysis conditions for fractionation. At these conditions the fat recovery was ?~81%; substantially more than previous attempts and the fatty acid profile stayed unchanged from the original larvae material. The protein solubility was ~57%, with a degree of hydrolysis of ~22%, and was on par with previous studies. The amino acid profile of the soluble proteins differed from the original larvae material with a slight decrease in the ratio of essential to total amino acids. The insoluble proteins were accounted for with the chitin. A washing-and-sieving step, as means to recover the insoluble proteins from the chitin is envisaged. Also, the spray drying of the protein hydrolysate produced and its functional properties allows for future investigation. This technology allows for higher margins to be made, both environmentally as well as financially, compared to the use of the ‘intact’ biomass.

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