scholarly journals Heat-Induced Interactions between Whey Protein and Inulin and Changes in Physicochemical and Antioxidative Properties of the Complexes

2019 ◽  
Vol 20 (17) ◽  
pp. 4089
Author(s):  
Wang ◽  
Wang ◽  
Sun ◽  
Sun ◽  
Guo
Keyword(s):  
Whey Protein ◽  
Structural Changes ◽  
Protein Profile ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Lower Surface ◽  
Surface Hydrophobicity ◽  
Antioxidative Properties ◽  
Dpph Scavenging ◽  
Far Ultraviolet

Whey protein and inulin at various weight ratios were dry heated at 60 °C for 5 days under relative humidity of 63%. The heated mixtures were found to have significant changes in browning intensity and zeta-potential compared to untreated mixture. Heated samples showed significantly lower surface hydrophobicity than untreated mixtures. Compared with untreated samples, dry-heated samples showed significantly higher 2,2-Diphenyl-1-Picrylhydrazyl (DPPH) scavenging ability with whey protein to inulin mass ratios of 1:2 and 1:3 and significantly higher 2,2′-Azinobis(2-Ethylbenzothiazoline-6-Sulfonate) (ABTS) scavenging abilities and oxygen radical absorbance capacity (ORAC) at all weight ratios. Dry heat-induced interactions between whey protein and inulin was confirmed by changes in Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE) protein profile, Fourier Transform Infrared Spectroscopy (FT-IR) and Far-ultraviolet Circular Dichroism (Far-UV CD) spectra. Dry heating caused physicochemical and structural changes of whey protein and therefore the complexes can be used to improve the antioxidative properties of the mixture under certain conditions.

scholarly journals EFFECTS OF HUMAN PLATELET LYSATES WITHOUT ADDITIONAL GROWTH FACTORS ON THE PROTEIN PROFILES OF HUMAN UMBILICAL VEIN ENDOTHELIAL CELL CULTURE MEDIA

2017 ◽  
Vol 10 (17) ◽  
pp. 54
Author(s):  
Hazriani Ra ◽  
Lisa Amir ◽  
Ratna Farida
Keyword(s):  
Culture Media ◽  
Umbilical Vein ◽  
Protein Profile ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Test Results ◽  
Control Groups ◽  
Cell Culture Media ◽  
Endothelial Cell Culture ◽  
Fetal Bovine

Objectives: The objective of this study is to evaluate the effect of HPLs with no additional GFs on the HUVEC protein profile. Methods: HUVEC cultures were examined in groups as follows: Fetal bovine serum (FBS), 2%-HPL with a GF, and 2%- and 5%-HPL without a GF which were analyzed with a sodium dodecyl sulfate-polyacrylamide gel electrophoresis test. Results: The intensity, thickness, and molecular weight of HUVEC band proteins cultured without a GF were not significantly different compared to the control groups (FBS or HPL with a GF). Conclusions: No difference was found in the HUVEC protein profile after they were cultured with FBS and HPLs, with or without GFs.

scholarly journals Simultaneous Ultrasound and Heat Enhance Functional Properties of Glycosylated Lactoferrin

Molecules ◽  
2020 ◽  
Vol 25 (23) ◽  
pp. 5774
Author(s):  
Zhipeng Li ◽  
Dexue Ma ◽  
Yiyang He ◽  
Siqi Guo ◽  
Fuguo Liu ◽  
...  
Keyword(s):  
Functional Properties ◽  
Maillard Reaction ◽  
Spatial Configuration ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Surface Hydrophobicity ◽  
Orthogonal Experimental Design ◽  
Maillard Reaction Products ◽  
Reaction Products ◽  
Ultrasound Assisted

Protein-polysaccharide covalent complexes exhibit better physicochemical and functional properties than single protein or polysaccharide. To promote the formation of the covalent complex from lactoferrin (LF) and beet pectin (BP), we enhanced the Maillard reaction between LF and BP by using an ultrasound-assisted treatment and studied the structure and functional properties of the resulting product. The reaction conditions were optimized by an orthogonal experimental design, and the highest grafting degree of 55.36% was obtained by ultrasonic treatment at 300 W for 20 min and at LF concentration of 20 g/L and BP concentration of 9 g/L. The formation of LF-BP conjugates was confirmed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared (FTIR) spectroscopy. Ultrasound-assisted treatment can increase the surface hydrophobicity, browning index, 1,1-diphenyl-2-picryl-hydrazyl (DPPH) and 2,2’-azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS) free radicals scavenging activity of LF due to the changes in the spatial configuration and formation of Maillard reaction products. The thermal stability, antioxidant activity and emulsifying property of LF were significantly improved after combining with BP. These findings reveal the potential application of modified proteins by ultrasonic and heat treatment.

scholarly journals Characterization of Proteins in the Outer Membrane Preparation of a Murine Pathogen, Helicobacter bilis

2001 ◽  
Vol 69 (5) ◽  
pp. 3502-3506 ◽  
Author(s):  
Zhongming Ge ◽  
Peter Doig ◽  
James G. Fox
Keyword(s):  
Outer Membrane ◽  
Wide Spectrum ◽  
Protein Profile ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cross Reactivity ◽  
Membrane Preparation ◽  
Laboratory Animals ◽  
Helicobacter Bilis ◽  
H Pylori

ABSTRACT Helicobacter bilis is a bacterial pathogen associated with multifocal hepatitis and inflammatory bowel disease in certain strains of mice. This bacterium colonizes the liver, bile, and lower intestine in mice and has also been isolated from a wide spectrum of laboratory animals. In this study, proteins present in the outer membrane preparation (OMP) of four H. bilis strains isolated from a mouse, a dog, a rat, and a gerbil were characterized and compared with that of Helicobacter pylori, a human gastric pathogen. All four H. bilis strains had similar OMP protein profiles that were distinct from those of H. pylori. Immunoblotting demonstrated that OMP proteins fromH. bilis and H. pylori have little cross-reactivity, except for their flagellins. Nine major immunogenic polypeptides were present in the H. bilis OMPs. By using two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis, five heat-modifiable proteins with molecular masses of 82, 66, 52, 47 and 37 kDa were identified. The N-terminal sequences of the 46- and 47-kDa OMP proteins had no homology with protein sequences available in public databases. These results indicate that H. bilis has a conserved, unique OMP protein profile that is distinct from those of H. pylori.

scholarly journals The population, protein profile and ultrastructure of Ascaridia galli in chicken treated using Areca catechu crude aqueous extract

2019 ◽  
Vol 44 (4) ◽  
pp. 392
Author(s):  
W. W. Mubarokah ◽  
W. Nurcahyo ◽  
J. Prastowo ◽  
K. Kurniasih
Keyword(s):  
Aqueous Extract ◽  
Protein Profile ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Anthelmintic Activity ◽  
Positive Control ◽  
Negative Control ◽  
Ascaridia Galli ◽  
Areca Catechu ◽  
Crude Aqueous Extract

The study aimed at investigating the population, the protein profile and the ultrastructure of adult worms in the intestine of domestic chicken treated using Areca catechu crude aqueous extract. Fifty domestic female chickens of 6 weeks of age were assigned to 5 groups. Group A (negative control) was not given any treatment and any drug. Groups B, C and D were given the treatment at the doses of 26 mg/mL, 53 mg/mL and 79 mg/mL, respectively. Group E (positive control) was given Pyrantel®. Necropsy was conducted to all of the chickens 14 days after the treatment. Adult worms were collected and counted. The worms used in Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE) and Scanning Electron Microscopy (SEM) were those collected from the jejunum of the chickens in the groups A, B and C. The biggest number of the worms was found in the jejunum. The results of electrophoresis showed that the dose 53 mg/mL gave fewer protein bands than the negative control (21:12 ratio), while the results of the SEM showed that there was cuticle damage and anterior labia abrasion at the dose of 53 mg/mL. The Areca catechu crude aqueous extract showed anthelmintic activity potential by reducing the number of the adult worms, lowering their protein profile and damaging the A. galli worms in the intestine.

scholarly journals Effects of High Intensity Ultrasound on Physiochemical and Structural Properties of Goat Milk β-Lactoglobulin

Molecules ◽  
2020 ◽  
Vol 25 (16) ◽  
pp. 3637
Author(s):  
Xinhui Zhou ◽  
Cuina Wang ◽  
Xiaomeng Sun ◽  
Zixuan Zhao ◽  
Mingruo Guo
Keyword(s):  
Thermal Stability ◽  
Structural Properties ◽  
High Intensity ◽  
Structural Changes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Goat Milk ◽  
High Intensity Ultrasound ◽  
Hydrophobicity Index ◽  
Β Lactoglobulin

This study aimed to compare the effects of high intensity ultrasound (HIU) applied at various amplitudes (20~40%) and for different durations (1~10 min) on the physiochemical and structural properties of goat milk β-lactoglobulin. No significant change was observed in the protein electrophoretic patterns by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Deconvolution and second derivative of the Fourier transform infrared spectra (FTIR) showed that the percentage of β-sheet of goat milk β-lactoglobulin was significantly decreased while those of α-helix and random coils increased after HIU treatment The surface hydrophobicity index and intrinsic fluorescence intensity of samples was enhanced and increased with increasing HIU amplitude or time. Differential scanning calorimetry (DSC) results exhibited that HIU treatments improved the thermal stability of goat milk β-lactoglobulin. Transmission electron microscopy (TEM) of samples showed that the goat milk β-lactoglobulin microstructure had changed and it contained larger aggregates when compared with the untreated goat milk β-lactoglobulin sample. Data suggested that HIU treatments resulted in secondary and tertiary structural changes of goat milk β-lactoglobulin and improved its thermal stability.

Rapid detection and initial characterization of genetic variants of human serum albumin

1991 ◽  
Vol 37 (7) ◽  
pp. 1221-1224 ◽  
Author(s):  
J Merle Sheat ◽  
Robert J Peach ◽  
Peter M George
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Genetic Variants ◽  
Gel Electrophoresis ◽  
Structural Changes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl

Abstract We have studied the detection and classification of genetic variants of human serum albumin by electrophoresis. Samples from 10 patients who were heterozygous for eight different albumin variants were studied by two methods. In agarose gel electrophoresis, each of these variants has an abnormal mobility and can be classified on the basis that structural changes at the N-terminus abolish 63Ni binding. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis of whole serum, glycosylated variants are easily detected because of their greater apparent molecular mass.

Oviductal fluid protein patterns in the rhesus monkey (Macaca mulatta) during the menstrual cycle

1992 ◽  
Vol 4 (2) ◽  
pp. 249 ◽  
Author(s):  
A Paliwal ◽  
B Malaviya ◽  
VP Kamboj
Keyword(s):  
Menstrual Cycle ◽  
Protein Profile ◽  
Periodic Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Blue Staining ◽  
Protein Patterns ◽  
Coomassie Blue Staining ◽  
Coomassie Blue ◽  
Oviductal Fluid

Oviducts were obtained from monkeys on Days 8, 14, 19 and 25 of the menstrual cycle and changes in the pattern of luminal fluid proteins were examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Densitometric analysis after periodic acid Schiff's reagent (PAS) and coomassie blue staining of the gels revealed 85 and 95 kDa proteins only up to Day 14 whereas a 130 kDa glycoprotein persisted up to Day 19 and reached a nadir at mid-menstrual cycle (Day 14). The absence of the 130 kDa glycoprotein in the serum and its presence in cytosolic preparations up to Day 19 suggest that it is of oviductal origin. The 130 kDa glycoprotein is of particular interest since it was present in the oviductal fluid during mid cycle, a period when the oviduct participates in gamete transport, fertilization and embryo development. The conclusion drawn from this study is that the protein profile of monkey oviductal fluid changes during the menstrual cycle.

A rapid method of species identification of wild chironomids (Diptera: Chironomidae) via electrophoresis of hemoglobin proteins in sodium dodecyl sulfate polyacrylamide gel (SDS–PAGE)

2014 ◽  
Vol 104 (5) ◽  
pp. 639-651 ◽  
Author(s):  
J.T. Oh ◽  
J.H. Epler ◽  
C.S. Bentivegna
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Protein Profile ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Head Capsule ◽  
Species Level ◽  
Polyacrylamide Gel ◽  
Taxonomic Identification ◽  
Sds Page ◽  
Dodecyl Sulfate

AbstractStudying aquatic benthic macroinvertebrates (BMIs) in the field requires accurate taxonomic identification, which can be difficult and time consuming. Conventionally, head capsule morphology has been used to identify wild larvae of Chironomidae. However, due to the number of species and possible damage and/or deformity of their head capsules, another supporting approach for identification is needed. Here, we provide hemoglobin (Hb) protein in hemolymph of chironomids as a new biomarker that may help resolve some of the ambiguities and difficulties encountered during taxonomic identification. Chironomids collected from two locations in Maine and New Jersey, USA were identified to the genus level and in some cases to the species-level using head capsule and body morphologies. The head capsule for a particular individual was then associated with a corresponding Hb protein profile generated from sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS–PAGE). Distinct Hb profiles were observed from one group (Thienemannimyia) and four genera (Chironomus, Cricotopus, Dicrotendipes, and Glyptotendipes) of chironomids. Several species were polymorphic, having more than one Hb profile and/or having bands of the same size as those of other species. However, major bands and the combination of bands could distinguish individuals at the genus and sometimes species-level. Overall, this study showed that Hb profiles can be used in combination with head capsule morphology to identify wild chironomids.

Whole-cell protein and ITS rDNA profiles as diagnostic tools to discriminate Fusarium avenaceum intraspecific variability and associated virulence

2009 ◽  
Vol 55 (2) ◽  
pp. 117-125 ◽  
Author(s):  
V. Vujanovic ◽  
S. Vidovic ◽  
M. R. Fernandez ◽  
P. Daida ◽  
D. Korber
Keyword(s):  
Protein Profile ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Intraspecific Variability ◽  
Fusarium Avenaceum ◽  
Cell Protein ◽  
Diagnostic Tools ◽  
Group Method ◽  
Head Blight ◽  
Sds Page

A total of 91 isolates of Fusarium avenaceum were regrouped into 15 phenotypes and 10 vegetative compatibility groups showing specific one-dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis (1-D SDS–PAGE) protein profiles and less-specific internal transcribed spacer rDNA profiles. Each isolate possessed reproducible signature protein bands. Indeed, the unweighted pair group method with arithmetic averages clustering revealed that the protein profile of each group of isolates correlated with fungus virulence. The use of SDS–PAGE offers a simple and sensitive technique for routine differentiation between pathogenic and nonpathogenic isolates within unknown F. avenaceum populations. The discovery has significant implications for risk assessment of cereal yield to ensure food and feed safety. This low-cost approach has the potential to be optimized and extended to a broad spectrum of Fusarium head blight pathogens.

scholarly journals Characterization of the yrbA Gene ofBacillus subtilis, Involved in Resistance and Germination of Spores

1999 ◽  
Vol 181 (16) ◽  
pp. 4986-4994 ◽  
Author(s):  
Hiromu Takamatsu ◽  
Takeko Kodama ◽  
Tatsuo Nakayama ◽  
Kazuhito Watabe
Keyword(s):  
Optical Density ◽  
Protein Profile ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Electron Microscopic Examination ◽  
Coat Proteins ◽  
Electron Microscopic ◽  
Consensus Sequences ◽  
Insertional Inactivation ◽  
Coat Layer

ABSTRACT Insertional inactivation of the yrbA gene ofBacillus subtilis reduced the resistance of the mutant spores to lysozyme. The yrbA mutant spores lost their optical density at the same rate as the wild-type spores upon incubation with l-alanine but became only phase gray and did not swell. The response of the mutant spores to a combination of asparagine, glucose, fructose, and KCl was also extremely poor; in this medium yrbA spores exhibited only a small loss in optical density and gave a mixture of phase-bright, -gray, and -dark spores. Northern blot analysis of yrbA transcripts in varioussig mutants indicated that yrbA was transcribed by RNA polymerase with ςE beginning at 2 h after the start of sporulation. The yrbA promoter was localized by primer extension analysis, and the sequences of the −35 (TCATAAC) and −10 (CATATGT) regions were similar to the consensus sequences of genes recognized by ςE. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of proteins solubilized from intact yrbA mutant spores showed an alteration in the protein profile, as 31- and 36-kDa proteins, identified as YrbA and CotG, respectively, were absent, along with some other minor changes. Electron microscopic examination ofyrbA spores revealed changes in the spore coat, including a reduction in the density and thickness of the outer layer and the appearance of an inner coat layer-like structure around the outside of the coat. This abnormal coat structure was also observed on the outside of the developing forespores of the yrbA mutant. These results suggest that YrbA is involved in assembly of some coat proteins which have roles in both spore lysozyme resistance and germination.

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