Modification of structural and functional properties of sunflower 11S globulin hydrolysates

The structural and functional properties such as solubility, emulsifying properties, foaming properties, oil binding capacity, and surface hydrophobicity of sunflower 11S globulin hydrolysates generated by Alcalase at hydrolysis time of 30, 60, 90, and 120 min were evaluated. Circular dichroism analysis showed the hydrolysates possessed a decreased α-helix and β-structure. The hydrolysates exhibited lower surface hydrophobicity. Hydrolysates with shorter hydrolysis time showed the higher emulsifying activity index, but the same emulsion stability and oil binding capacity compared to the original 11S globulin. The longer hydrolysis resulted in lower foaming and emulsion stability. Thus it was demonstrated that by controlling the hydrolysis time of sunflower 11S globulin, hydrolysate with a desirable functional properties can be obtained.

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Characterization of Asian swamp eel (Monopterus sp.) protein hydrolysate functional properties prepared using Alcalase® enzyme

Food Research ◽

10.26656/fr.2017.4(1).205 ◽

2019 ◽

Vol 4 (1) ◽

pp. 207-215 ◽

Cited By ~ 1

Author(s):

N.R.A. Halim ◽

Norizah Mhd Sarbon

Keyword(s):

Functional Properties ◽

Protein Hydrolysate ◽

Binding Capacity ◽

Foaming Properties ◽

Protein Supplements ◽

Fish Meat ◽

Hydrophobic Amino Acids ◽

Asian Swamp Eel ◽

Water Holding ◽

Oil Binding

Fish protein hydrolysates have good nutritional properties and thus can be obtained by treatment of fish meat with enzymes under controlled conditions. It is used for texturing, gelling, foaming, emulsification, protein supplements, flavor enhancers, and beverage stabilizers. The aims of this study were to prepare eel protein hydrolysate (EPH) prepared using Alcalase® enzyme and characterize its physicochemical properties. The structural, solubility, emulsifying and foaming properties, water holding and oil binding capacity of EPH were examined. Structural results obtained found that the presence of hydrophilic and hydrophobic amino acids together with the presence of aromatic groups. There were no significant differences (p>0.05) between EPH at different pH levels in solubility. However, in terms of emulsifying and foaming properties, EPH showed significant differences (p<0.05) at different pH levels, while water holding capacity showed significant differences (p<0.05) at different EPH concentrations. There were no significant differences (p>0.05) in the oil binding capacities of EPH at different concentrations. The functional properties possessed by EPH showed that it has potential as an emulsifier and stabilizer in food products, playing an important role in the food industry.

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Improving the Functionality of Proso Millet Protein and Its Potential as a Functional Food Ingredient by Applying Nitrogen Fertiliser

Foods ◽

10.3390/foods10061332 ◽

2021 ◽

Vol 10 (6) ◽

pp. 1332

Author(s):

Honglu Wang ◽

Dongmei Li ◽

Chenxi Wan ◽

Yan Luo ◽

Qinghua Yang ◽

...

Keyword(s):

Functional Properties ◽

Amino Acid Content ◽

Control Group ◽

Foaming Properties ◽

Food Ingredient ◽

Nitrogen Fertiliser ◽

Proso Millet ◽

Structural And Functional Properties ◽

High Amino Acid ◽

Β Sheet

Nitrogen is required for proso millet growth and has a critical influence on yield and quality. However, the effect of nitrogen fertilisation on proso millet protein properties remains unclear. This study aimed to investigate how nitrogen fertiliser treatment (180 kg/hm2) affects the structural and functional properties of proso millet protein. In comparison with the control group (N0), nitrogen fertiliser treatment loosened the dense structure of the protein and presented a larger particle size. Nitrogen treatment did not change the main subunit composition, and β-sheet and α-helix were the main secondary structures of proso millet protein based on Fourier transform infrared spectroscopy. In addition, nitrogen fertiliser treatment improved the content of hydrophobic amino acids and β-sheet proportion from proso millet protein, and high water/oil absorption capacity and thermal stability was observed, but the solubility, emulsion stability and foaming properties from proso millet protein decreased. Proso millet proteins exhibited high amino acid content and good functional properties, including solubility, foaming capacity and emulsifying properties, especially the w139 variety. Results show that proso millet protein has great potential for food applications. The above results provide useful information for the food industry to determine emerging gluten-free protein resources.

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Chicken skin gelatine as an alternative to pork and beef gelatines

Potravinarstvo Slovak Journal of Food Sciences ◽

10.5219/1022 ◽

2019 ◽

Vol 13 (1) ◽

pp. 224-233 ◽

Cited By ~ 1

Author(s):

Petr Mrázek ◽

Pavel Mokrejš ◽

Robert Gál ◽

Jana Orsavová

Keyword(s):

Functional Properties ◽

Binding Capacity ◽

Water Holding Capacity ◽

Poultry Meat ◽

Foaming Properties ◽

Extraction Temperature ◽

Chicken Skin ◽

Foaming Capacity ◽

Water Holding ◽

By Products

Poultry meat-processing industry produces considerably large amounts of by-products (such as chicken skins, heads, feathers, viscera, bones and legs) containing significant volumes of proteins, particularly collagen. One of the possibilities of advantageous utilization of these under-used by-products can be their application as a raw material rich in collagen for preparation of gelatine, a partial hydrolysate of collagen. In the present study, chicken skins obtained as a by-product from the chicken-breast processing were purified from non-collagen proteins, pigments and fats. Collagen was treated with proteolytic enzymes and the gelatine extraction was performed in distilled water at temperatures of 40, 50, 60, 70 and 80 °C during the constant extraction time of 60 min. The influence of the technological conditions on gelatine functional properties including viscosity, clarity, water holding and fat binding capacity, emulsifying and foaming properties was explored. Certain functional properties of prepared gelatines were significantly affected by the extraction temperature, while on some other properties the extraction temperature had no significant effect. Viscosity of prepared chicken skin gelatines was in the range from 3 to 5.7 mPa.s, clarity from 1.5 to 2%, water holding capacity from 3.8 to 5.6 mL.g-1, fat binding capacity from 0.9 to 1.3 mL.g-1, emulsion capacity from 35 to 50%, emulsion stability from 73 to 88%, foaming capacity from 18 to 61% and finally foaming stability was from 4 to 39%. Chicken skin gelatines were compared with commercial food grade pork and beef gelatines. Prepared chicken skin gelatines showed better viscosity, fat binding capacity and foaming stability than mammalian gelatines, while water holding capacity, emulsifying stability and foaming capacity were not as good as in beef and pork gelatines. Emulsifying capacity was comparable with commercial gelatines. Therefore, chicken skin gelatine has the potential as an alternative to traditional gelatines from mammalian sources, such as pork or beef bones and skins.

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Effects of Baicalein and Chrysin on the Structure and Functional Properties of β-Lactoglobulin

Foods ◽

10.3390/foods11020165 ◽

2022 ◽

Vol 11 (2) ◽

pp. 165

Author(s):

Ang Li ◽

Lei Chen ◽

Weijie Zhou ◽

Junhui Pan ◽

Deming Gong ◽

...

Keyword(s):

Hydrogen Bond ◽

Molecular Docking ◽

Functional Properties ◽

Sulfhydryl Group ◽

Surface Hydrophobicity ◽

Dynamics Simulation ◽

Foaming Properties ◽

Hydrogen Bond Formation ◽

Simulation Techniques ◽

Β Lactoglobulin

Two flavonoids with similar structures, baicalein (Bai) and chrysin (Chr), were selected to investigate the interactions with β-lactoglobulin (BLG) and the influences on the structure and functional properties of BLG by multispectral methods combined with molecular docking and dynamic (MD) simulation techniques. The results of fluorescence quenching suggested that both Bai and Chr interacted with BLG to form complexes with the binding constant of the magnitude of 105 L·mol−1. The binding affinity between BLG and Bai was stronger than that of Chr due to more hydrogen bond formation in Bai–BLG binding. The existence of Bai or Chr induced a looser conformation of BLG, but Chr had a greater effect on the secondary structure of BLG. The surface hydrophobicity and free sulfhydryl group content of BLG lessened due to the presence of the two flavonoids. Molecular docking was performed at the binding site of Bai or Chr located in the surface of BLG, and hydrophobic interaction and hydrogen bond actuated the formation of the Bai/Chr–BLG complex. Molecular dynamics simulation verified that the combination of Chr and BLG decreased the stability of BLG, while Bai had little effect on it. Moreover, the foaming properties of BLG got better in the presence of the two flavonoids compounds and Bai improved its emulsification stability of the protein, but Chr had the opposite effect. This work provides a new idea for the development of novel dietary supplements using functional proteins as flavonoid delivery vectors.

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Effects of High-Pressure Homogenization at Different Pressures on Structure and Functional Properties of Oyster Protein Isolates

International Journal of Food Engineering ◽

10.1515/ijfe-2018-0009 ◽

2018 ◽

Vol 14 (4) ◽

Cited By ~ 5

Author(s):

Cuiping Yu ◽

Fan Wu ◽

Yue Cha ◽

Yuting Qin ◽

Ming Du

Keyword(s):

Particle Size ◽

High Pressure ◽

Secondary Structure ◽

Zeta Potential ◽

Functional Properties ◽

Surface Hydrophobicity ◽

Random Coil ◽

Foaming Properties ◽

High Pressure Homogenization ◽

Protein Profiles

Abstract Oyster protein isolate (OPI) suspensions (6.19 % ± 0.82 %, w/v) were treated by high-pressure homogenization (HPH) at 0 (control), 20, 40, 60, 80 or 100 MPa for three cycles. Protein profiles, secondary structure, free sulfhydryl, surface hydrophobicity, particle size distribution, zeta-potential, solubility, water and oil holding capacity (OHC), emulsifying and foaming properties of the obtained suspensions were analyzed. The results showed that HPH treatment did not cause changes in protein profiles of OPI, but caused changes in secondary structure, content of α-helix decreased but content of β-turn and random coil increased significantly (P < 0.05). Free sulfhydryl and surface hydrophobicity all increased significantly (P < 0.05) after HPH treatment, indicating that tertiary and quaternary structures changed. Functional properties of OPI significantly (P < 0.05) improved after HPH treatment, such as zeta-potential (from −12.67 to −33.57 mV), solubility (from 20.24 % to 57.99 %), OHC (from 981.77 % to 1229.40 %), foaming ability (from 17.50 % to 35.00 %), foaming stability (from 44.49 % to 66.60 %), emulsifying activity index (from 8.87 to 17.06 m2/g) and emulsion stability index (from 14.65 to 41.68 min). At 60 MPa and 80 MPa, the improvements were more remarkable. However, HPH treatment significantly (P < 0.05) decreased particle size (from 200–500 nm to 0–200 nm) and water holding capacity (from 341.15 % to 216.96 %). These improvements were closely related to structural changes and reduction of particle size. Application of different pressures affected functional properties of OPI. These results could provide information for determining HPH applying condition in OPI modification.

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Characterizing the Structural and Functional Properties of Soybean Protein Extracted from Full-Fat Soybean Flakes after Low-Temperature Dry Extrusion

Molecules ◽

10.3390/molecules23123265 ◽

2018 ◽

Vol 23 (12) ◽

pp. 3265 ◽

Cited By ~ 3

Author(s):

Wenjun Ma ◽

Fengying Xie ◽

Shuang Zhang ◽

Huan Wang ◽

Miao Hu ◽

...

Keyword(s):

Functional Properties ◽

Soy Protein ◽

Activity Index ◽

Soybean Protein ◽

Stability Index ◽

Extrusion Temperature ◽

Emulsifying Activity ◽

Protein Isolates ◽

Soy Protein Isolates ◽

Structural And Functional Properties

The soy protein isolates (SPI) extracted from different extruded full-fat soybean flakes (FFSF), and their conformational and functional properties were characterized. Overall, the free thiol (SH) content of SPI increased when the extrusion temperature was below 80 °C and decreased at higher temperatures. Soy glycinin (11S) showed higher stability than β-conglycinin (7S) during extrusion. Results also indicated that the increase in some hydrophobic groups was due to the movement of hydrophobic groups from the interior to the surface of the SPI molecules at extrusion temperatures from 60 to 80 °C. However, the aggregation of SPI molecules occurred at extrusion temperatures of 90 and 100 °C, with decreasing levels of hydrophobic groups. The extrusion temperature negatively affected the emulsifying activity index (EAI); on the other side, it positively affected the emulsifying stability index (ESI), compared to unextruded SPI.

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High-Pressure Homogenization Pre-Treatment Improved Functional Properties of Oyster Protein Isolate Hydrolysates

Molecules ◽

10.3390/molecules23123344 ◽

2018 ◽

Vol 23 (12) ◽

pp. 3344 ◽

Cited By ~ 4

Author(s):

Yue Cha ◽

Fan Wu ◽

Henan Zou ◽

Xiaojie Shi ◽

Yidi Zhao ◽

...

Keyword(s):

Particle Size ◽

High Pressure ◽

Zeta Potential ◽

Functional Properties ◽

Potential Surface ◽

Activity Index ◽

Surface Hydrophobicity ◽

High Pressure Homogenization ◽

Emulsifying Activity ◽

Pre Treatment

The effects of HPH (high-pressure homogenization) pre-treatment on the functional properties of OPIH (oyster protein isolates hydrolysates) were studied. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis profiles, solubility, particle size distribution, zeta potential, surface hydrophobicity, emulsifying activity index and microstructure of emulsions were analyzed. Results indicated that HPH pre-treatment increased the accessibility of OPI to trypsin hydrolysis, resulting in decease in particle size, increase in solubility, absolute zeta potential, surface hydrophobicity and emulsifying activity index. In addition, HPH pre-treated OPIH emulsions became more uniform and the particle size of droplets decreased. These results revealed that HPH pre-treatment has the potential to modify the functional properties of OPIH.

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Structural and Functional Properties of Heat-processed Soybean Flour: Effect of Proteolytic Modification

Food Science and Technology International ◽

10.1177/1082013209350347 ◽

2009 ◽

Vol 15 (5) ◽

pp. 453-463 ◽

Cited By ~ 11

Author(s):

C. Radha ◽

V. Prakash

Keyword(s):

Functional Properties ◽

Structural Changes ◽

Chemical Properties ◽

Surface Hydrophobicity ◽

Soy Flour ◽

Heat Processing ◽

Enzymatic Modification ◽

Defatted Soy Flour ◽

Physico Chemical ◽

Structural And Functional Properties

Heat processing of soybeans alters its structural behavior, solubility, and in turn the functional properties. Heat-processed soy flour was prepared by autoclaving the defatted soy flour at 121 °C at 15 psi. The effect of enzymatic modification on the structural changes and functional properties of heat-processed soy flour was investigated. The combination of heat processing and enzymatic modification was carried out in two ways: (1) enzymatic modification followed by autoclaving and (2) autoclaving followed by enzymatic modification. Defatted soy flour (control), autoclaved soy flour, enzyme-modified flour, enzyme-modified and then autoclaved flour, autoclaved and then enzyme-modified flour were analyzed for physico-chemical and functional properties. Molecular weight profile of the protein was altered depending on the nature of treatments. Structural studies showed that enzymatic modification gave a porous type morphology to the particles. Enzymatic modification of autoclaved soy flour increased its surface hydrophobicity to 3136±400 units from 600±100 units of autoclaved soy flour. The results indicated that enzymatic modification of autoclaved soy flour increased its acid solubility (pH 4—4.5) from 17% to 56% over a control value of 24%. The foaming capacity of the enzyme-modified and then autoclaved soy flour was 80% while that of the autoclaved and then enzyme-modified flour was 42%. The soy flour that was autoclaved and then enzyme modified showed better emulsifying properties (174 mL oil/g flour) than the flour that was enzyme-modified and then autoclaved. The modified soy flour based on its functional and physico-chemical properties should find application in many food systems.

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Isolation and Characterization of The Functional Properties of The Major Protein Fraction from Nyamplung (Calophyllum inophyllum)

Indonesian Food and Nutrition Progress ◽

10.22146/jifnp.114 ◽

2014 ◽

Vol 13 (1) ◽

pp. 17

Author(s):

Muhammad Prima Putra ◽

Pudji Hastuti

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Functional Properties ◽

Binding Capacity ◽

Major Protein ◽

Water Binding ◽

Water Emulsion ◽

Calophyllum Inophyllum ◽

Isolation And Characterization ◽

Oil Binding

Defatted nyamplung (Calophyllum inophyllum) seeds as by-products of oil extraction is a rich source of protein. In order to evaluate its potential as value-added of nyamplung seeds, nyamplung proteins were isolated by solubilization-precipitation method at pH 3 and 5. The obtaining protein isolates were characterized with respect to their functional properties, including water binding capacity, oil binding capacity, foaming capacity, foaming stability, emulsifying activity, emulsifying stability, gelation capacity, and amino acid composition. The results show that nyamplung protein could be considered as high protein quality because essential amino acids leucine (4.39 %), proline (4.22 %), valine (3.34 %), aspartic acid (3.23 %) and lysine (3.34 %) were found to be the major amino acids. Polar amino acids were higher than non-polar amino acid (1.7 times). With the consequence in higher ratio of water binding capacity to oil binding capacity (2.7 times) and high value of hydrophile-lypophile balance. In general, the isolated protein from precipitation at pH 3 (IP3) was found to have better functional properties than that being precipitated at pH (IP5), and showed excellent in water binding, emulsifying, gelation and foaming properties. In conclusion, IP3 can be utilized as high quality proteins and emulsifier in oil in water emulsion system.

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Structural and Functional Changes in Ultrasonicated Oyster Protein Isolates

International Journal of Food Engineering ◽

10.1515/ijfe-2018-0190 ◽

2019 ◽

Vol 15 (3-4) ◽

Cited By ~ 1

Author(s):

Cuiping Yu ◽

Fan Wu ◽

Yue Cha ◽

Henan Zou ◽

Yingnan Guo ◽

...

Keyword(s):

Particle Size ◽

Functional Properties ◽

Activity Index ◽

Protein Solubility ◽

Stability Index ◽

Protein Isolates ◽

Complex Needs ◽

Functional Changes ◽

Structural And Functional Properties ◽

Water Holding

AbstractStructural and functional changes in ultrasonicated oyster protein isolates (OPI) were investigated. Ultrasound treatments were carried out with probe (20 kHz) at 200, 400 and 600 W for 15 and 30 min. The results showed that functional properties of OPI significantly improved after sonication. Absolute zeta potential and protein solubility increased by 18.40 mV and 82.5 % at 600 W for 15 min. Oil holding capacity, emulsifying activity index, emulsion stability index, foaming ability and foaming stability increased by 300 %, 15.23 m2/g, 9.24 min, 23.9 % and 14.8 % at 600 W for 30 min. However, ultrasound treatment significantly (P < 0.05) decreased particle size and water holding capacity. The conformation of OPI became stretched and unfolded after sonication. Functional improvements resulted from stretched and unfolded conformation and reduction of particle size. Controlled condition of ultrasound can produce OPI with distinct structural and functional properties, which could meet the complex needs of manufactured food products in food industry, but further study is needed to understand the specific mechanism.

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