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.

Structural changes and allergenic properties of β-lactoglobulin upon exposure to high-intensity ultrasound

2012 ◽  
Vol 56 (12) ◽  
pp. 1894-1905 ◽  
Author(s):  
Dragana Stanic-Vucinic ◽  
Marija Stojadinovic ◽  
Marina Atanaskovic-Markovic ◽  
Jana Ognjenovic ◽  
Hans Grönlund ◽  
...  
Keyword(s):  
High Intensity ◽  
Structural Changes ◽  
High Intensity Ultrasound ◽  
Β Lactoglobulin

scholarly journals Increased Tissue Penetration of Doxorubicin in Pressurized Intraperitoneal Aerosol Chemotherapy (PIPAC) after High-Intensity Ultrasound (HIUS)

2019 ◽  
Vol 2019 ◽  
pp. 1-6 ◽  
Author(s):  
Veria Khosrawipour ◽  
Sören Reinhard ◽  
Alice Martino ◽  
Tanja Khosrawipour ◽  
Mohamed Arafkas ◽  
...  
Keyword(s):  
Intraperitoneal Chemotherapy ◽  
High Intensity ◽  
Structural Damage ◽  
Structural Changes ◽  
Therapeutic Option ◽  
Tissue Penetration ◽  
High Intensity Ultrasound ◽  
Tissue Samples ◽  
Thin Sections ◽  
Peritoneal Tissue

Background. High‐intensity ultrasound (HIUS) has been studied for the past two decades as a new therapeutic option for solid tumor direct treatment and a method for better chemotherapy delivery and perfusion. This treatment approach has not been tested to our knowledge in peritoneal metastatic therapy, where limited tissue penetration of intraperitoneal chemotherapy has been a main problem. Both liquid instillations and pressurized aerosols are affected by this limitation. This study was performed to evaluate whether HIUS improves chemotherapy penetration rates. Methods. High-intensity ultrasound (HIUS) was applied for 0, 5, 30, 60, 120, and 300 seconds on the peritoneal tissue samples from fresh postmortem swine. Samples were then treated with doxorubicin via pressurized intraperitoneal aerosol chemotherapy (PIPAC) under 12 mmHg and 37°C temperature. Tissue penetration of doxorubicin was measured using fluorescence microscopy on frozen thin sections. Results. Macroscopic structural changes, identified by swelling of the superficial layer of the peritoneal surface, were observed after 120 seconds of HIUS. Maximum doxorubicin penetration was significantly higher in peritoneum treated with HIUS for 300 seconds, with a depth of 962.88 ± 161.4 μm (p < 0.05). Samples without HIUS had a penetration depth of 252.25 ± 60.41. Tissue penetration was significantly increased with longer HIUS duration, with up to 3.8-fold increased penetration after 300 sec of HIUS treatment. Conclusion. Our data indicate that HIUS may be used as a method to prepare the peritoneal tissue for intraperitoneal chemotherapy. Higher tissue penetration rates can be achieved without increasing chemotherapy concentrations and preventing structural damage to tissue using short time intervals. More studies need to be performed to analyze the effect of HIUS in combination with intraperitoneal chemotherapy.

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.

Preparing the peritoneal surface for intraperitoneal chemotherapy using high-intensity ultrasound (HIUS): Investigation of technical feasibility, safety and possible limitations.

2020 ◽  
Vol 38 (15_suppl) ◽  
pp. e16045-e16045
Author(s):  
Veria Khosrawipour ◽  
Piotr Frelkiewicz ◽  
Sören Reinhard ◽  
Jakub Nicpon ◽  
Tanja Khosrawipour ◽  
...  
Keyword(s):  
Intraperitoneal Chemotherapy ◽  
High Intensity ◽  
Structural Changes ◽  
Ex Vivo ◽  
Abdominal Cavity ◽  
Swine Model ◽  
High Intensity Ultrasound ◽  
Technical Feasibility ◽  
Tissue Samples ◽  
Peritoneal Surface

e16045 Background: The penetration of chemotherapeutic drugs into metastatic peritoneal nodules remains at levels well below 1 mm, thus significantly limiting the antitumor effect of intraperitoneal chemotherapy (IPC). Recently, high-Intensity ultrasound (HIUS) has been discovered as a potential tool to improve peritoneal diffusion rates. Despite promising preliminary data, basic aspects regarding its technical feasibility, safety and possible limitations remain unclear. This study aims to enhance our current understanding of HIUS and test its applicability using an ex-vivo swine model. Methods: Three postmortem swine were subject to laparotomy with consecutive lavage with 0.9%NaCl saline and HIUS application. For this purpose, a large HIUS radiating pen was introduced into the abdominal cavity and HIUS was applied on two of the four abdominal quadrants for 300 seconds each at an output power of 70 W, 50 % amplitude and 20 kHz frequency. Following the procedure, small intestinal tissue samples were removed for further analyses. Results: In all specimen, peritoneal and subperitoneal layers showed structural changes only visible on a microscopic level. The peritoneal layer was transformed into a mash-like structure while the subperitoneal layer (depth of 142 +/- 28 µm) exhibited microcavities and vascular detachment from surrounding tissues. No bowel rupture or vascular perforations were observed. Conclusions: Our data indicate that HIUS is a technically feasible add-on procedure for IPC with measurable microscopic changes on the peritoneal surface and no apparent bowel toxicity. Pretreatment of the abdominal cavity with HIUS could significantly improve IPC efficacy. Further studies are required to optimize and evaluate this novel approach.

Effect of high-intensity ultrasound on the compositional, physicochemical, biochemical, functional and structural properties of canola (Brassica napus L.) protein isolate

2019 ◽  
Vol 121 ◽  
pp. 947-956 ◽  
Author(s):  
Nitzia Thalía Flores-Jiménez ◽  
José Armando Ulloa ◽  
Judith Esmeralda Urías Silvas ◽  
José Carmen Ramírez Ramírez ◽  
Petra Rosas Ulloa ◽  
...  
Keyword(s):  
Brassica Napus ◽  
Structural Properties ◽  
High Intensity ◽  
Protein Isolate ◽  
High Intensity Ultrasound ◽  
Brassica Napus L ◽  
L Protein

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 Contribution of Chemical Modifications and Conformational Epitopes to IgE Binding by Ara h 3

Foods ◽  
2018 ◽  
Vol 7 (11) ◽  
pp. 189 ◽  
Author(s):  
Scott Dyer ◽  
Jacqueline Nesbit ◽  
Beatriz Cabanillas ◽  
Hsiaopo Cheng ◽  
Barry Hurlburt ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Secondary Structure ◽  
Disulfide Bonds ◽  
Structural Changes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cd Spectroscopy ◽  
Chemical Modifications ◽  
Ige Binding ◽  
Ara H 3

Roasting is known to change the allergenic properties of peanuts. To study these observations at a molecular level, the relationship of IgE binding to the structure of Ara h 3 from raw and roasted peanuts was assessed. Ara h 3 (A3) was purified from raw (R), light roast (LR) and dark roast (DR) peanuts, the purity was assessed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and the secondary structures were compared with circular dichroism (CD) spectroscopy. In order to understand the contribution of structure to IgE binding, the R A3 was partially denatured (PD) by heat treatment (65 °C for 2 h), subjected to CD spectroscopy and IgE spot blot analysis with sera from peanut- allergic individuals. While we observed that the secondary structure of purified A3 from R and LR peanut in solution was affected by the reduction of disulfide bonds and heat treatment when purified from the peanut following the roasting process, only small alterations were seen in the secondary structure. The purified LR A3 bound higher levels of IgE than the RA3. CD spectroscopy of PD A3 revealed a reduction in the percentage of alpha helices, and serum IgE binding. Therefore, while A3 purified from roasted peanuts did not show significant changes in secondary structure, it showed higher IgE binding than R A3. Therefore, the higher IgE binding to LR A3 was more likely to be due to chemical modifications than structural changes. However, a decrease in the IgE binding was seen if R A3 was deliberately unfolded, indicating that the structure played an important role in IgE binding to A3.

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