Study on Mechanism of Cross-Linking of Peanut Protein Isolate Modified with Transglutaminase

2012 ◽  
Vol 550-553 ◽  
pp. 1304-1308 ◽  
Author(s):  
Qing Jie Sun ◽  
Liu Xiong ◽  
Xiang Hui Bu ◽  
Yan Liu
Keyword(s):  
Ir Spectra ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Isolate ◽  
Peanut Protein ◽  
Cross Linking ◽  
Banding Patterns ◽  
Peanut Protein Isolate ◽  
Sds Page ◽  
Ft Ir

The mechanism of cross-linking of peanut protein isolate (PPI) modified with transglutaminase was investigated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier Transformation Infrared (FT-IR) spectra. SDS-PAGE banding patterns indicated that the contents of arachin and conarachin after transglutaminase (TGase) modification were decreased and high molecular weight polymers were formed. SDS-PAGE banding patterns also suggested that cross-linking effects were accomplished in the presence of transglutaminase and the main component participating in cross-linking was arachin. The representative FT-IR spectra of arachin, conarachin modified with TGase treatment appeared the sharp peak at 1680~1630cm-1 region, which showed that intramolecular cross-linking was occurred, respectively. Compared with FT-IR spectra of arachin, conarachin modified with TGase treatment, the spectra of PPI modified with TGase treatment appeared two characteristic absorption at 1546.29cm-1 and 1330.75cm-1, suggesting that cross-linking was occurred between arachin and conarachin and the ε-(γ-glutamyl) isopeptide bond generated.

scholarly journals Effects of Graphene Oxide on the Structure and Properties of Regenerated Wool Keratin Films

Polymers ◽  
2018 ◽  
Vol 10 (12) ◽  
pp. 1318 ◽  
Author(s):  
Bo Li ◽  
Jinbo Yao ◽  
Jiarong Niu ◽  
Jianyong Liu ◽  
Le Wang ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Graphene Oxide ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Test Results ◽  
Chemical Methods ◽  
Sds Page ◽  
Mechanism Of Interaction ◽  
Ft Ir ◽  
Ir And Raman

Much research has focused on improvement of the structural and mechanical properties of regenerated keratin materials by physical or chemical methods in recent years. In this research, regenerated keratin materials were modified with graphene oxide (GO). The properties of modified keratin films and the mechanism of interaction between GO and keratin macromolecules were studied. The SEM and XRD test results showed that the orientation of keratin macromolecules could be effectively improved by GO, which favored improvement of the keratin material’s crystallinity and made the films more uniform and compact. The thermal stability and mechanical properties of GO-modified keratin films were also improved significantly. At the same time, the reaction mechanism between keratin and GO materials was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), FT-IR, and Raman spectroscopy. It was shown that there was no chemical reaction between GO and keratin molecules, and the interaction between them was mainly via hydrogen bonding and van der Waals forces.

scholarly journals Digestibility of β-lactoglobulin following cross-linking by trametes versicolor laccase and apple polyphenols

2011 ◽  
Vol 76 (6) ◽  
pp. 847-855 ◽  
Author(s):  
Ziyad Tantoush ◽  
Luka Mihajlovic ◽  
Bojana Kravic ◽  
Jana Ognjenovic ◽  
Ratko Jankov ◽  
...  
Keyword(s):  
Nutritional Value ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cross Linking ◽  
Allergenic Potential ◽  
Sds Page ◽  
Molecular Masses ◽  
Quercetin Glycosides ◽  
Phenolic Extract ◽  
Β Lactoglobulin

?-Lactoglobulin (BLG) is an important nutrient of dairy products and an important allergen in cow?s milk allergy. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an apple phenolic extract (APE) and to characterize the obtained products for their digestibility by pepsin and pancreatin. The composition of the apple phenolics used for cross-linking was determined by LC-ESE-MS. The apple phenolic extract contained significant amounts of quercetin glycosides, catechins and chlorogenic acid. The laccase cross-linked BLG in the presence of apple phenolics. The polymerization rendered the protein insoluble in the reaction mixture. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the cross-linking reaction mixture revealed a heterogeneous mixture of high molecular masses (cross-linked BLG), with a fraction of the BLG remaining monomeric. Enzymatic processing of BLG by laccase and apple polyphenols as mediators can decrease the bi-phasal pepsin- pancreatin digestibility of the monomeric and cross-linked protein, thus decreasing its nutritional value. In addition, reduced BLG digestibility can decrease its allergenic potential. Apple polyphenols can find usage in the creation of new, more functional food products, designed to prevent obesity and hypersensitivity-related disorders.

scholarly journals SDS-PAGE Characterisation of Crude Seed and Leaf Proteins in Corchorus Species

2015 ◽  
Vol 7 (2) ◽  
pp. 177-183
Author(s):  
Christiana Adeyinka AJALA ◽  
Joseph Akintade MORAKINYO
Keyword(s):  
Protein Separation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Electrophoretic Study ◽  
Single Linkage ◽  
Banding Patterns ◽  
Leaf Proteins ◽  
Sds Page ◽  
Single Linkage Cluster ◽  
Linkage Cluster

Crude protein separation was carried out for Corchorus incisifolious, Corchorus aestuans, Corchorus tridens and Corchorus olitorious using Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE). Plants were collected both from wild and cultivated sites and samples included leaves and seeds for the electrophoretic study. Distinct polymorphism in electrophoretic banding patterns of seed and leaf proteins following SDS- PAGE was observed in the four Corchorus species studied. Forty- two polypeptide bands were observed in the seed and a total of eleven polypeptide bands were observed in the leaves of the Corchorus species studied. The electrophoretic study revealed protein bands with various intensities ranging from high, to low and faint. The results showed that there was variation in both the seed and leaf proteins of the Corchorus species studied. A dendrogram constructed based on the Single Linkage Cluster Analysis (SLCA) clustering method revealed three major clusters for seeds. Cluster I consisted of C. incisifolious and C. aestuans, cluster II consisted of C. tridens, while cluster III consisted of C. olitorious. The leaf protein extracts were grouped into two clusters, cluster one containing C. incisifolious and C. aestuans, while the other contained C. tridens and C. olitorious.

The αEC domain of human fibrinogen-420 is a stable and early plasmin cleavage product

Blood ◽  
2000 ◽  
Vol 95 (7) ◽  
pp. 2297-2303 ◽  
Author(s):  
Dianne Applegate ◽  
Lara Stoike Steben ◽  
Kathe M. Hertzberg ◽  
Gerd Grieninger
Keyword(s):  
Gel Electrophoresis ◽  
Degradation Products ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cleavage Product ◽  
The Other ◽  
Cross Linking ◽  
Human Fibrinogen ◽  
Western Blots ◽  
Sds Page

Abstract Human fibrinogen-420, (Eβγ)2, was isolated from plasma and evaluated for its ability to form clots and for its susceptibility to proteolysis. Clotting parameters, including cross-linking of subunit chains, of this subclass and of the more abundant fibrinogen-340 (βγ)2, were found to be similar, suggesting little impact of the unique EC domains of fibrinogen-420 on coagulation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) analysis of plasmic digestion patterns revealed production from fibrinogen-420 of the conventional fibrinogen degradation products, X, Y, D, and E, to be comparable to that from fibrinogen-340 in all respects except the presence of at least 2 additional cleavage products that were shown by Western blot analysis to contain the EC domain. One was a stable fragment (ECX) comigrating with a 34-kd yeast recombinant EC domain, and the other was an apparent precursor. Their release occurred early, before that of fragments D and E. Two bands of the same mobility and antibody reactivity were found in Western blots of plasma collected from patients with myocardial infarction shortly after the initiation of thrombolytic therapy.

Film Formation and Structural Characterization of Silk of the Hornet Vespa simillima xanthoptera Cameron

2005 ◽  
Vol 60 (11-12) ◽  
pp. 906-914 ◽  
Author(s):  
Tsunenori Kameda ◽  
Katsura Kojima ◽  
Mitsuhiro Miyazawa ◽  
Seita Fujiwara
Keyword(s):  
Film Formation ◽  
Pure Water ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Molecular Weights ◽  
Sds Page ◽  
Ft Ir ◽  
Α Helix ◽  
Β Sheet

We extracted silk produced by the larva of the hornet Vespa simillima xanthoptera Cameron from its nest. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the extracted hornet silk showed four major components with molecular weights between 35 and 60 kDa. The main amino acid components of the hornet silk protein were Ala (33.5%), Ser (16.9%), Asp (8.5%) and Glu (8.1%). The hornet silk could be dissolved in hexafluoroisopropyl alcohol (HFIP) at 25 °C without incurring molecular degradation. A transparent film of hornet silk was obtained readily by the formation of a cast upon drying of the hornet silk in the HFIP solution. Residual HFIP solvent was removed from the film by extraction with pure water. Solid-state 13C NMR and FT-IR measurements revealed that the secondary structures of hornet silk proteins in the native state consisted of coexisting α-helix and β-sheet conformations. The β-sheet to α-helix ratio, which was changed by processing, was mainly responsible for the silk’s thermostability.

scholarly journals Identification of barley cultivars using SDS-PAGE electrophoresis

1992 ◽  
Vol 1 (1) ◽  
pp. 73-82
Author(s):  
Janne Roininen ◽  
Eero Nissilä ◽  
Matti Puolimatka ◽  
Seppo Pulli
Keyword(s):  
Seed Storage Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Hordeum Vulgare L ◽  
Banding Patterns ◽  
Breeding Lines ◽  
Barley Cultivars ◽  
Sds Page ◽  
Single Seeds

Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) was applied to cultivar identification. Three different extractions methods were used to extract and fractionate the seed storage protein subunits from crushed single seeds of barley (Hordeum vulgare L.). Fifty-four genotypes including breeding lines and released cultivars were analysed and grouped according to the variation found in their protein banding patterns. In the first extraction, eight genotypes showed unique hordein subunit composition whilst remainder fell into 11 groups of 2 to 8. The other two extractions were carried out to characterize those genotypes producing identical banding patterns when using the first method. Relative mobility (REM) values for hordein bands were determined. Genetic background was found to strongly effect the determination of hordein composition of barley genotypes. Those genotypes with largely common ancestry showed often similar hordein composition and were difficult to identify whereas genotypes possessing unique hordein banding patterns had clearly exceptional pedigree. The effect of the row-type on hordein banding pattern was not clear as both two-row and many-row barleys were found to produce identical patterns. Intra-cultivar hordein polymorfism was found in three cultivars.

scholarly journals Characterization of Protease Soluble Collagen (PSC) From Milkfish Scales (Chanos chanos)

2019 ◽  
Vol 8 (3) ◽  
pp. 245-254
Author(s):  
Nia Lutfiana ◽  
◽  
Suharti Suharti ◽  
Evi Susanti ◽  
◽  
...  
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Collagen Type I ◽  
Differential Scanning Calorimetric ◽  
Type I ◽  
Denaturation Temperature ◽  
Soluble Collagen ◽  
Sds Page ◽  
Ft Ir

The aim of this study was to characterize protease soluble collagen (PSC) obtained from milkfish scales, extraction using protease from proteolytic bacteria HTcUM7.1 isolate. The characterization included Fourier Transform Infra Red (FT-IR) spectra, Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE) profile, Field Emission Scanning Electron Microscopy (FESEM), denaturation temperature by Differential Scanning Calorimetric (DSC) and solubility. The resulting PSC from milkfish scales has white color, fiber with a length of about 20-60 µm, FTIR spectra and SDS-PAGE profile showed that PSC was collagen Type I and denaturation temperature was 145.48 °C, with maximum solubility at pH 1-3 and 1-2 % NaCl. Its high denaturation temperature value allows the collagen to be applied in the fields of medicines and cosmetics.

The αEC domain of human fibrinogen-420 is a stable and early plasmin cleavage product

Blood ◽  
2000 ◽  
Vol 95 (7) ◽  
pp. 2297-2303 ◽  
Author(s):  
Dianne Applegate ◽  
Lara Stoike Steben ◽  
Kathe M. Hertzberg ◽  
Gerd Grieninger
Keyword(s):  
Gel Electrophoresis ◽  
Degradation Products ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cleavage Product ◽  
The Other ◽  
Cross Linking ◽  
Human Fibrinogen ◽  
Western Blots ◽  
Sds Page

Human fibrinogen-420, (Eβγ)2, was isolated from plasma and evaluated for its ability to form clots and for its susceptibility to proteolysis. Clotting parameters, including cross-linking of subunit chains, of this subclass and of the more abundant fibrinogen-340 (βγ)2, were found to be similar, suggesting little impact of the unique EC domains of fibrinogen-420 on coagulation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) analysis of plasmic digestion patterns revealed production from fibrinogen-420 of the conventional fibrinogen degradation products, X, Y, D, and E, to be comparable to that from fibrinogen-340 in all respects except the presence of at least 2 additional cleavage products that were shown by Western blot analysis to contain the EC domain. One was a stable fragment (ECX) comigrating with a 34-kd yeast recombinant EC domain, and the other was an apparent precursor. Their release occurred early, before that of fragments D and E. Two bands of the same mobility and antibody reactivity were found in Western blots of plasma collected from patients with myocardial infarction shortly after the initiation of thrombolytic therapy.

Electrophoretic Heterogeneity of Lipopolysaccharides of Actinobacillus actinomycetemcomitans

1988 ◽  
Vol 67 (3) ◽  
pp. 574-576 ◽  
Author(s):  
C.I. Hoover
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Epidemiological Studies ◽  
Actinobacillus Actinomycetemcomitans ◽  
Relative Mobility ◽  
Banding Patterns ◽  
Sds Page ◽  
Staining Techniques ◽  
Serotype B ◽  
Phenol Water

Electrophoretic banding patterns of lipopolysaccharides (LPS), as observed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), have proved to be useful in studies relating LPS structure to virulence and as epidemiological markers. In this report, LPS of Actinobacillus actinomycetemcomitans from outer membrane fractions and hot phenol-water extracts were analyzed by SDS-PAGE and LPS-specific silver-staining techniques. Both intra- and inter-strain heterogeneity of A. actinomycetemcomitans LPS was observed. Twelve strains of A. actinomycetemcomitans, representative of the three described serotypes, were assigned to LPS subtypes based on the relative mobility of their most rapidly migrating LPS band. All three serotype a strains (29523, aB75, and GA3), two (29524 and SAC11A) of five serotype b strains, and two (aB67 and SAC5A) of four serotype c strains were assigned to LPS subtype I. The three remaining serotype b strains (29522, Y4, and JP2) were assigned to LPS subtype II, and the remaining two serotype c strains (SAC6A and SAC12A) were assigned to LPS subtype III. LPS subtyping may serve as an adjunct or alternative to serotyping in epidemiological studies.

Sign in / Sign up

Export Citation Format

Share Document