scholarly journals Effect of Hydrolysis on Tannin and Carotenoid Contents, and Antioxidant Activity of Pouteria campechiana

2021 ◽  
Vol 4 (1) ◽  
pp. 1
Author(s):  
Hien Xuan Tran ◽  
Huong Lien Huynh ◽  
Thanh Trung Nguyen
Keyword(s):  
Antioxidant Activity ◽  
Food Industry ◽  
Enzyme Concentration ◽  
Scientific Data ◽  
Hydrolysis Time ◽  
Ic50 Value ◽  
Hydrolysis Temperature ◽  
Medicinal Properties ◽  
Highly Correlated ◽  
Hydrolysis Conditions

The medicinal properties of Pouteria campechiana fruit in Vietnam currently have not been studied much. This study was conducted to evaluate hydrolysis's effect on the carotenoid, tannin, and antioxidant activity through the correlation between IC50 and TPC values of Pouteria campechiana extract. This study examined hydrolysis conditions, such as enzyme type, enzyme concentration, temperature, and hydrolysis time. Experimental results showed that at pectinase enzyme concentration of 0.6 wt%, cellulase enzyme concentration of 0.6 wt%, at hydrolysis temperature of 600C, and 65 minutes for hydrolysis, the study found carotenoid of 115.14±4.14 (µg/g) and tannin of 45.88±2.37 (mgTAE/g)in the extract. IC50 value (7.82±0.21 mg/mL) and TPC content were highly correlated (R2=0.98). This study's results contributed to the provision of valuable scientific data on Pouteria campechiana fruit, especially for the food industry

scholarly journals Enzymatic Hydrolysis of Defatted Antheraea pernyi (Lepidoptera: Saturniidae) Pupa Protein by Combined Neutral Protease Yield Peptides With Antioxidant Activity

2021 ◽  
Vol 21 (2) ◽  
Author(s):  
Shuhui Ma ◽  
Xuejun Li ◽  
Yongxin Sun ◽  
Rui Mi ◽  
Yajie Li ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Enzyme Concentration ◽  
Activity Assay ◽  
Antioxidant Peptides ◽  
Hydrolysis Time ◽  
Antheraea Pernyi ◽  
Hydrolysis Temperature ◽  
High Antioxidant Activity ◽  
Hydrolysis Of ◽  
Neutral Proteases

Abstract In this study, peptides were prepared from defatted Antheraea pernyi (Lepidoptera: Saturniidae) pupa protein via hydrolysis with combined neutral proteases. Single-factor tests and response surface methodology (RSM) were used to determine the optimal hydrolysis condition suitable for industrial application. Optimal hydrolysis of the defatted pupa protein was found to occur at an enzyme concentration of 4.85 g/liter, a substrate concentration of 41 g/liter, a hydrolysis temperature of 55°C, and a hydrolysis time of 10 h and 40 min. Under these conditions, the predicted and actual rates of hydrolysis were 45.82% and 45.75%, respectively. Peptides with a molecular weight of less than 2,000 Da accounted for 90.5% of the total peptides generated. Some of the peptides were antioxidant peptides as revealed by sequencing and functional analysis. The antioxidant activity of the mixed peptides was subsequently confirmed by an antioxidant activity assay. The results showed that peptides with high antioxidant activity could be obtained from the hydrolysis of A. pernyi pupa protein.

scholarly journals Optimization of Oyster (Crassostrea talienwhanensis) Protein Hydrolysates Using Response Surface Methodology

Molecules ◽  
2020 ◽  
Vol 25 (12) ◽  
pp. 2844 ◽  
Author(s):  
Xueqin Wang ◽  
Huahua Yu ◽  
Ronge Xing ◽  
Song Liu ◽  
Xiaolin Chen ◽  
...  
Keyword(s):  
Response Surface Methodology ◽  
Response Surface ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Enzyme Concentration ◽  
Degree Of Hydrolysis ◽  
Hydrolysis Time ◽  
Hydrolysis Temperature ◽  
Hydrolysis Conditions ◽  
Different Response

Oyster (Crassostrea talienwhanensis) protein was hydrolyzed by trypsin to produce peptides with different response values, and response surface methodology (RSM) was applied to optimize the hydrolysis conditions. The highest degree of hydrolysis (DH) of the oyster peptide (OP) was obtained at an enzyme concentration of 1593.2 U/g, a pH of 8.2, a hydrolysis temperature of 40.1 °C, a hydrolysis time of 6.0 h, and a water/material ratio of 8.2. The greatest hydroxyl-radical-scavenging activity of OP was obtained at an enzyme concentration of 1546.3 U/g, a pH of 9.0, a hydrolysis temperature of 50.2 °C, a hydrolysis time of 5.1 h, and a water/material ratio of 5.6. The largest branched-chain amino acid (BCAA) content of OP was obtained at an enzyme concentration of 1323.8 U/g, a pH of 8.3, a hydrolysis temperature of 41.7 °C, a hydrolysis time of 6.7 h, and a water/material ratio of 4.8. The three experimental values were significantly in agreement with the predicted values within the 95% confidence interval. Furthermore, ultrafiltration and chromatographic methods were used to purify the OP, and 13 peptides that were rich in Lys, Arg, His, and Thr were identified by LC-MS/MS. The results of this study offer different optimum hydrolysis conditions to produce target peptides from oyster protein by using RSM, and this study provide a theoretical basis for the high-value utilization of oyster protein.

scholarly journals Hydrolysate from Mussel Mytilus galloprovincialis Meat: Enzymatic Hydrolysis, Optimization and Bioactive Properties

Molecules ◽  
2021 ◽  
Vol 26 (17) ◽  
pp. 5228
Author(s):  
Sara A. Cunha ◽  
Rita de Castro ◽  
Ezequiel R. Coscueta ◽  
Manuela Pintado
Keyword(s):  
Antioxidant Activity ◽  
Enzymatic Hydrolysis ◽  
Mytilus Galloprovincialis ◽  
Target Market ◽  
Hydrolysis Time ◽  
Bioactive Properties ◽  
Hydrolysis Temperature ◽  
Market Criteria ◽  
Enzyme Ratio ◽  
Production Conditions

Mussel production generates losses and waste since their commercialisation must be aligned with target market criteria. Since mussels are rich in proteins, their meat can be explored as a source of bioactive hydrolysates. Thus, the main objective of this study was to establish the optimal production conditions through two Box–Behnken designs to produce, by enzymatic hydrolysis (using subtilisin and corolase), hydrolysates rich in proteins and with bioactive properties. The factorial design allowed for the evaluation of the effects of three factors (hydrolysis temperature, enzyme ratio, and hydrolysis time) on protein/peptides release as well as antioxidant and anti-hypertensive properties of the hydrolysates. The hydrolysates produced using the optimised conditions using the subtilisin protease showed 45.0 ± 0.38% of protein, antioxidant activity via ORAC method of 485.63 ± 60.65 µmol TE/g of hydrolysate, and an IC50 for the inhibition of ACE of 1.0 ± 0.56 mg of protein/mL. The hydrolysates produced using corolase showed 46.35 ± 1.12% of protein, antioxidant activity of 389.48 ± 0.21 µmol TE/g of hydrolysate, and an IC50 for the inhibition of ACE of 3.7 ± 0.33 mg of protein/mL. Mussel meat losses and waste can be used as a source of hydrolysates rich in peptides with relevant bioactive properties, and showing potential for use as ingredients in different industries, such as food and cosmetics, contributing to a circular economy and reducing world waste.

Study on Hydrolysis Conditions of Lactobacillus bulgaricus on Casein Sodium by Method of Response Surface and the Antioxidant Activity of Hydrolysates

2014 ◽  
Vol 884-885 ◽  
pp. 535-539
Author(s):  
Zhen Yan Liu ◽  
Wen Qin Yang ◽  
Han Liu ◽  
Jie Zhang ◽  
Chuan Gang Zang ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Response Surface ◽  
Ph Value ◽  
Negative Impact ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Lactobacillus Bulgaricus ◽  
Cultivation Time ◽  
Hydrolysis Temperature ◽  
Hydrolysis Conditions

In order to study the ability ofLactobacillus bulgaricushydrolyzed protein, using casein sodium as substrate, the content of free amino acid and relative ORAC value were used as the index optimization. The conditions including: hydrolysis temperature, cultivation time,Lactobacillus bulgaricusdosage and pH values were investigated by single-factor experiment. In this paper we studied the hydrolysis conditions ofLactobacillus bulgaricuson casein sodium by the Box-Behnken response surface and the optimal hydrolysis temperature, cultivation time,Lactobacillus bulgaricusdosage and pH value were determined to be 43 °C, 36 h, 25 OD/ml, and pH 6.6, respectively. The optimum value of response surface is 857.75 mg/l. In addition, the analysis of relative ORAC value of response surface showed that there is no direct relationship between the degree of protein hydrolysis and radical scavenging activity, namely as extensive hydrolysis could have a negative impact on the antioxidant activity.

Optimization of Enzymatic Hydrolysis Conditions for Preparation of Gingko Peptides from Ginkgo Nuts

2012 ◽  
Vol 8 (1) ◽  
Author(s):  
Hanju Sun ◽  
Zhe Chen ◽  
Peng Wen ◽  
Hong Lei ◽  
Juan Shi ◽  
...  
Keyword(s):  
Reaction Temperature ◽  
Substrate Concentration ◽  
Orthogonal Experiment ◽  
Enzyme Concentration ◽  
Neutral Protease ◽  
Degree Of Hydrolysis ◽  
Single Factor ◽  
Hydrolysis Time ◽  
Initial Ph ◽  
Hydrolysis Conditions

Ginkgo nuts were used as raw material and peptides were prepared in turn with Neutral protease and Flavourzyme. In single-factor experiments of Neutral protease, conditions of temperature, pH, enzyme concentration and substrate concentration were optimized in term of degree of hydrolysis (DH). Based on the results of single-factor experiments, an orthogonal experiment (L9(3)4) was conducted to optimize the hydrolysis conditions of Neutral protease. The results showed that enzyme concentration, substrate concentration, reaction temperature and initial pH were the main variables that influenced DH. The highest DH was obtained when hydrolysis time, reaction temperature, initial pH, enzyme amount and substrate concentration were 4 h, 45 oC, 7.0, 1.8 mg/mL and 0.02 g/mL, respectively. Subsequently, the resulting solution was further hydrolyzed with Flavourzyme. Initial pH, temperature, time and enzyme concentration were optimized in term of DH. Finally, another orthogonal experiment (L9(3)4) was conducted to get the best enzymatic conditions of Flavourzyme, and enzyme concentration, initial pH, temperature and time were used as factors. The results showed that when Flavourzyme concentration, reaction temperature, initial pH and hydrolysis time were 9.0 mg/mL, 50 oC, 7.0 and 5 h, respectively, DH was the highest. The final degree of hydrolysis was 22.56%.

scholarly journals ANTIOXIDATIVE ACTIVITY AND PHYTOCHEMISTRY PROFILE OF HIBISCUS SABDARIFFA HERB EXTRACTS

2019 ◽  
pp. 29-32
Author(s):  
QOTRUNNADA FITROTUNNISA ◽  
ADE ARSIANTI ◽  
NADZILA ANINDYA TEJAPUTRI ◽  
FONA QORINA
Keyword(s):  
Antioxidant Activity ◽  
Ethyl Acetate ◽  
Hibiscus Sabdariffa ◽  
Ic50 Value ◽  
Dpph Method ◽  
Medicinal Properties ◽  
Phytochemical Profile ◽  
Tlc Analysis ◽  
Layer Chromatography ◽  
Herb Extracts

Objective: Hibiscus sabdariffa, known as Roselle, is a widely-cultivated herb in Indonesia and has been consumed as an herbal drink due to its medicinal properties. The purpose of this research is to identify the antioxidant activity and phytochemical profile of Hibiscus sabdariffa. Methods: The Hibiscus sabdariffa samples were extracted and macerated with three different organic solvents: ethyl acetate, ethanol, and n-hexane. These extracts were then analyzed using thin layer chromatography (TLC) and phytochemical tests to identify the extracts’ secondary metabolites. The extracts’ antioxidant activity was evaluated using the 2,2-diphenyl-1-picrylhydrazyl (DPPH) method. Results: The phytochemistry tests were positive for glycosides, alkaloids, steroids, triterpenoids, tannins, and flavonoids. The TLC analysis revealed that the extracts containing two to three organic compounds. The ethanol Hibiscus sabdariffa extracts with an IC50 value 103.63 ppm showed stronger antioxidant activity than the ethyl acetate extract. Conclusion: Ethanol Hibiscus sabdariffa extracts may be a potential source of natural antioxidant.

Preparation of Microcrystalline Cellulose from Cotton Linter Ethanol Pulp

2011 ◽  
Vol 295-297 ◽  
pp. 653-658
Author(s):  
Shan Shan Liu ◽  
Gui Gan Fang ◽  
Yong Jun Deng ◽  
Qiang Wang
Keyword(s):  
Particle Size ◽  
Factorial Design ◽  
Microcrystalline Cellulose ◽  
Experimental Results ◽  
Cotton Linter ◽  
Hydrolysis Time ◽  
Liquor Ratio ◽  
Hydrolysis Temperature ◽  
Hydrolysis Conditions

The hydrolysis trials of produce microcrystalline cellulose from cotton linter ethnaol pulp by hydrochloric were investigated. Based on 23 factorial design, fifteen operations were performed by varying S/L, T and t (S/L: solid to liquor ratio, T: hydrolysis temperature, t: hydrolysis time). The charecteristic of product was analyzed by X-RD, SEM and laser granularity distributing apparatus, and compared with commercial MCC. The experimental results indicated that MCC yield and particle size were influenced significantly by those factors. The optimal hydrolysis conditions was S/L=1:7, T=60°C and t=40min, which can resulted MCC yield of 75.3% and size of 21.21µm. Crystallinity of MCC is 63.96% and displayed as rod-shape.

scholarly journals A Novel Gelatinase from Marine Flocculibacter collagenilyticus SM1988: Characterization and Potential Application in Collagen Oligopeptide-Rich Hydrolysate Preparation

Marine Drugs ◽  
2022 ◽  
Vol 20 (1) ◽  
pp. 48
Author(s):  
Jian Li ◽  
Jun-Hui Cheng ◽  
Zhao-Jie Teng ◽  
Xia Zhang ◽  
Xiu-Lan Chen ◽  
...  
Keyword(s):  
Potential Application ◽  
Domain Architecture ◽  
Bone Collagen ◽  
Bovine Bone ◽  
Hydrolysis Time ◽  
Collagen Peptide ◽  
Enzyme Substrate ◽  
Hydrolysis Temperature ◽  
Merops Database ◽  
Hydrolysis Conditions

Although the S8 family in the MEROPS database contains many peptidases, only a few S8 peptidases have been applied in the preparation of bioactive oligopeptides. Bovine bone collagen is a good source for preparing collagen oligopeptides, but has been so far rarely applied in collagen peptide preparation. Here, we characterized a novel S8 gelatinase, Aa2_1884, from marine bacterium Flocculibacter collagenilyticus SM1988T, and evaluated its potential application in the preparation of collagen oligopeptides from bovine bone collagen. Aa2_1884 is a multimodular S8 peptidase with a distinct domain architecture from other reported peptidases. The recombinant Aa2_1884 over-expressed in Escherichia coli showed high activity toward gelatin and denatured collagens, but no activity toward natural collagens, indicating that Aa2_1884 is a gelatinase. To evaluate the potential of Aa2_1884 in the preparation of collagen oligopeptides from bovine bone collagen, three enzymatic hydrolysis parameters, hydrolysis temperature, hydrolysis time and enzyme-substrate ratio (E/S), were optimized by single factor experiments, and the optimal hydrolysis conditions were determined to be reaction at 60 ℃ for 3 h with an E/S of 400 U/g. Under these conditions, the hydrolysis efficiency of bovine bone collagen by Aa2_1884 reached 95.3%. The resultant hydrolysate contained 97.8% peptides, in which peptides with a molecular weight lower than 1000 Da and 500 Da accounted for 55.1% and 39.5%, respectively, indicating that the hydrolysate was rich in oligopeptides. These results indicate that Aa2_1884 likely has a promising potential application in the preparation of collagen oligopeptide-rich hydrolysate from bovine bone collagen, which may provide a feasible way for the high-value utilization of bovine bone collagen.

scholarly journals Production of fish seasoning powder from snakehead meat (Channa striata) by applying Alcalase and Flavourzyme enzyme mixture

2020 ◽  
Vol 19 (02) ◽  
pp. 43-49
Keyword(s):  
Moisture Content ◽  
Amino Acid Content ◽  
Hydrolysis Time ◽  
Ammonia Content ◽  
Fish Meat ◽  
Enzyme Mixture ◽  
Sensory Score ◽  
Hydrolysis Temperature ◽  
Channa Striata ◽  
Hydrolysis Conditions

Fish hydrolysate was produced from snakehead meat by applying an enzyme mixture consisting of Alcalase and Flavourzyme with a ratio of 1:3; hydrolysis temperature 55oC; pH 6.5 - 6.9. The results showed that the ratio of enzyme mixture to fish meat of 0.2% and hydrolysis time of 26 h were the optimal hydrolysis conditions. Fish hydrolysate had highest peptide content (26.4 g/L) and nitrogen amino acid content (10.6 g/L), and lowest nitrogen ammonia content (0.257 g/L). Sensory score, protein content, recovery yield and moisture content of fish seasoning powder were 18.9; 17.1%; 42.5% and 4.88%, respectively by mixing radish solution and fish hydrolysate at the ratio of radish solution to fish hydrolysate of 25%:40% and drying at 60oC for 72 h. The product still remained good sensory quality. The moisture content and total aerobic bacteria of product were at acceptable level after 4 weeks stored at ambient temperature.

scholarly journals ENZYMATIC SACHARIFICATION OF ALKALINE PRETREATED RICE STRAW BY CELLULASE FROM CELLULOSIMICROBIUM SP. MP1

2021 ◽  
Vol 58 (6A) ◽  
pp. 244
Author(s):  
Dao Thi Thanh Xuan ◽  
Le Thanh Ha ◽  
Phi Quyet Tien
Keyword(s):  
Technological Parameter ◽  
Enzymatic Saccharification ◽  
Enzyme Concentration ◽  
Reducing Sugar ◽  
Alkaline Pretreatment ◽  
Cellulose Content ◽  
Liquid Ratio ◽  
Hydrolysis Time ◽  
Saccharification Yield ◽  
Hydrolysis Conditions

The effects of different physical and technological parameter such as time, substrate to liquid ratio, enzyme concentration, temperature, and pH on enzymatic saccharification of alkaline pretreated straw cellulose were studied. For alkaline pretreatment, the straw was incubated with 10 % NaOH at ratio 1:20 (w/v) at 90 °C for 1 hour. After the alkaline pretreatment the cellulose content increased from 50.2 % (w/w) to 67.3 % (w/w). Enzyme used for saccharification of treated and untreated straw  was produced from Cellulosimicrobium sp MP1 which was isolated from termite gut. Results from research showed that the highest percentage of saccharification of alkaline pretreated straw was 69.91 %, corresponding to 10.58 mg/mL of reducing sugar. The hydrolysis conditions for reaching this highest saccharification yield were: temperature of 55 ºC, substrate to liquid ratio of 2 g/100 mL, enzyme concentration of 37.5 U/g, pH of 5.5 and hydrolysis time of 48 hours.

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