Evaluation of Hardness and Retrogradation of Cooked Rice Based on Its Pasting Properties Using a Novel RVA Testing

With rice being one of the most important crops worldwide, rapid and objective quality evaluation methods based on physicochemical measurements of rice are necessary. We compared the pasting properties of various rice samples using three different heating and cooling programs (maximum temperatures were 93, 120, and 140 °C, respectively) in a newly developed high-temperature-type Rapid Visco Analyzer (RVA , RVA 4800). Furthermore, we investigated the relationship between the different pasting properties measured by the three programs, with starch microstructure measured by iodine scanning analysis, the physical properties of the cooked rice measured by a Tensipresser after 2 h at 25 °C or after 24 h at 6 °C, and prolamin ratio measured by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The consistency value (final viscosity–minimum viscosity) yielded by a new program of maintenance for 2 min at 120 °C using RVA 4800 had a higher positive correlation with retrograded surface hardness H1(R) (r = 0.92), retrograded overall hardness H2(R) (r = 0.90), and the absorbance at λmax (Aλmax) of cooked rice (r = 0.88) and resistant starch (r = 0.80) than those by the conventional program at 93 °C. We developed estimation formulae for H1(R) for various kinds of rice, of which the determination coefficient was 0.86. It led to an easy and rapid assay method for the cooking properties of the various rice samples.

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Characterization of proteoglycans from the calcified matrix of bovine bone

Biochemical Journal ◽

10.1042/bj2240059 ◽

1984 ◽

Vol 224 (1) ◽

pp. 59-66 ◽

Cited By ~ 55

Author(s):

A Franzén ◽

D Heinegård

Keyword(s):

Molecular Mass ◽

Core Protein ◽

Chondroitin Sulphate ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Sedimentation Coefficient ◽

Sedimentation Equilibrium ◽

Assay Method ◽

Enzyme Linked Immunosorbent Assay ◽

Bovine Bone

The proteoglycans characterized were those isolated from the calcified matrix of mature bovine bone [Franzén & Heinegård (1984) Biochem. J. 224, 47-58]. The average molecular mass of the bone proteoglycan is 74 600 Da, determined by sedimentation-equilibrium centrifugation in 4M-guanidinium chloride. Its sedimentation coefficient (s0(20),w) is 3.04 S. The apparent Mr of its core protein is 46 000, estimated by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of the chondroitinase ABC-digested proteoglycan. A more likely molecular mass of the core protein is 30 000 Da, as calculated from the molecular mass and the protein content (40%) of the proteoglycan. The bone proteoglycan contains one or probably two chondroitin sulphate chains each with a molecular mass (weight-average) of 33 700 Da and several oligosaccharides both of the N-glycosidically and the O-glycosidically linked type. Antibodies against the homogeneous bone proteoglycans were raised in rabbits. An e.l.i.s.a. (enzyme-linked immunosorbent assay) method was developed that allowed specific quantification of bone proteoglycans at nanogram levels. The specificity of the antibodies was tested by using the e.l.i.s.a. method. The bone proteoglycan showed partial cross-reactivity with the small proteoglycan of cartilage. The antibodies were used to localize immunoreactivity of bone proteoglycans by indirect immunofluorescence in frozen sections of foetal bovine epiphysial growth plate. The fluorescence was entirely found in the primary spongiosa, and no fluorescence was found among the hypertrophied chondrocytes or in the region of provisional calcification.

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Characteristics of Physicochemical Properties of Chalky Grains of Japonica Rice Generated by High Temperature during Ripening

Foods ◽

10.3390/foods11010097 ◽

2021 ◽

Vol 11 (1) ◽

pp. 97

Author(s):

Sumiko Nakamura ◽

Ayaka Satoh ◽

Masaki Aizawa ◽

Ken’ichi Ohtsubo

Keyword(s):

High Temperature ◽

Correlation Coefficients ◽

Pasting Properties ◽

High Ratio ◽

Japonica Rice ◽

Rice Grains ◽

Estimation Formula ◽

Cooking Properties ◽

Damage Degree ◽

Rice Samples

Global warming has caused devastating damage to starch biosynthesis, which has led to the increase in chalky grains of rice. This study was conducted to characterize the qualities of chalky rice grains and to develop the estimation formulae for their quality damage degree. We evaluated the chalkiness of 40 Japonica rice samples harvested in 2019, in Japan. Seven samples with a high ratio of chalky rice grains were selected and divided into two groups (whole grain and chalky grain). As a results of the various physicochemical measurements, it was shown that the surface layer hardness (H1) of cooked rice grains from chalky grains was significantly lower, and their overall hardness was significantly lower than those from the whole grains. In addition, α- and β-amylase activities, and sugar contents of the chalky rice grains were significantly higher than those of the whole rice grains. The developed estimation formula for the degree of retrogradation of H1 based on the α-amylase activities and pasting properties, showed correlation coefficients of 0.84 and 0.81 in the calibration and validation tests, respectively. This result presents the formula that could be used to estimate and to characterize the cooking properties of the rice samples ripened under high temperature.

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Conjugation strategies on functionalized iron oxide nanoparticles as a malaria vaccine delivery system

Bionatura ◽

10.21931/rb/2021.06.03.20 ◽

2021 ◽

Vol 3 (3) ◽

pp. 2009-2016

Author(s):

Aswan Al-Abboodi ◽

Hussain A. Mhouse Alsaady ◽

Shaima R. Banoon ◽

Mohammed Al-Saady

Keyword(s):

Infectious Diseases ◽

Magnetite Nanoparticles ◽

Proteolytic Enzymes ◽

Binding Capacity ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Plasmodium Yoelii ◽

Assay Method ◽

Nanoparticle Suspension

Vaccination has been used effectively to protect from infectious diseases and non-infectious diseases such as cancer and allergies. Different forms of particulate arrangements, including nanoparticles, virus-like particles (VLPs), and virosomes, have been built recently depending on the type of pathogen to be targeted. The ability to conjugate the recombinant Plasmodium yoelii, 19-kDa C-terminal fragment of merozoite surface protein 1 (PyMSP119) on the surface of superparamagnetic magnetite nanoparticles (SPIONs) was explored as a new technique of enhancing vaccination against malaria. Different conjugation strategies were performed to correlate the effects of nanoparticle chemistry surfaces to bind later with the malaria protein. (SPIONs) were prepared by chemical coprecipitation method and coated with 3-aminopropyltriethoxysilane (APTS) alone (as a surface coater), or with both APTS and polyethylene glycol (PEG) (as a shield to protect the malaria protein from proteolytic enzymes) by using a modified silanisation method. X-ray powder diffraction (XRD, Philips Model) patterns indicated that the SPIONs were of high purity with an inverse spinal structure. Fourier Transform Infrared Spectroscopy (FTIR) was collected using PerkinElmer Spectrum 100 Series; spectra of uncoated and coated magnetite nanoparticles confirmed that the silane layer had been coated on the surface Fe3O4. The SPIONs were superparamagnetic as investigated by Vibrating Sample Magnetometry (VSM, Princeton Applied Research, model ISS) and relatively stable in aqueous phase at room temperature and could also be quickly recovered from suspension using an external magnet. Introduce the carboxyl groups onto the SPIONs surfaces, resulting in a relatively high protein binding capacity onto the nanoparticle surfaces. The bare particles had a mean size of around 20 nm with a relatively narrow size distribution. 82% of African Green Monkey fibroblast (COS-7) were alive in nanoparticle suspension using the MTT assay method. The quantity of protein explicitly bound to particles was determined using Sodium Dodecyl Sulfate (SDS) - Polyacrylamide Gel Electrophoresis (PAGE). SDS–PAGE. When the conjugation blend was prepared in EDC, there was approximately 100% binding between PyMSP119 and the Fe3O4-COOH particles because no protein band was apparent at the expected molecular weight for PyMSP119 (45 kDa). The current study investigates the theory that the gradual, persistent release of the malaria antigen may stimulate and maintain an elevated level of immune response for an extended period in vivo, which will be the scope of future work.

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One-step purification of chicken growth hormone from a crude pituitary extract by use of a monoclonal immunoadsorbent

Journal of Endocrinology ◽

10.1677/joe.0.1180381 ◽

1988 ◽

Vol 118 (3) ◽

pp. 381-387 ◽

Cited By ~ 64

Author(s):

L. R. Berghman ◽

J. van Beeumen ◽

E. Decuypere ◽

E. R. Kühn ◽

F. Vandesande

Keyword(s):

Monoclonal Antibodies ◽

High Performance ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Reversed Phase ◽

Molecular Forms ◽

Assay Method ◽

One Step ◽

Purification Protocol

ABSTRACT The immunization of mice with an affinity-purified glycoprotein preparation from chicken pituitary tissue yielded several monoclonal antibodies towards the recently described glycosylated variant of chicken GH. As all these antibodies recognize the classical (non-glycosylated) GH molecule equally well, they provide a suitable tool for the development of both a specific immunoadsorbent and an assay method. This paper deals with the surprising purification power of the immunoadsorbent that was produced with one of the monoclonal antibodies. The resulting preparation was more than 99% pure as assessed by reversed phase high-performance liquid chromatography and sodium dodecyl sulphate-polyacrylamide gel electrophoresis, so that no further purification steps were needed before the determination of the amino acid sequence of the material. The efficiency of the purification protocol as determined by a homologous, monoclonal antibody-based radioimmunoassay was virtually absolute. Moreover, the affinity-purified GH preparation was a mixture representing the multiple molecular forms of pituitary chicken GH, including both oligomeres and glycosylated GH. The purified preparations were finally used to demonstrate the hepatic 5′-monodeiodinase-stimulating activity of GH in the chicken embryo (results not shown), in order to prove that the biological activity of the molecule had not been damaged by elution from the immunoadsorbent. J. Endocr. (1988) 118, 381–387

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Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

Thrombosis and Haemostasis ◽

10.1055/s-0038-1646313 ◽

1992 ◽

Vol 68 (05) ◽

pp. 534-538 ◽

Cited By ~ 5

Author(s):

Nobuhiko Yoshida ◽

Shingi Imaoka ◽

Hajime Hirata ◽

Michio Matsuda ◽

Shinji Asakura

Keyword(s):

Molecular Weight ◽

Sodium Dodecyl Sulfate ◽

Gel Electrophoresis ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Tetraacetic Acid ◽

Fibrin Monomer ◽

Sds Page ◽

Thrombotic Tendency ◽

Chain Variant

SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).

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The Recovery of Factor VIII from Fresh-Frozen, Indated and Outdated Human Plasma

Thrombosis and Haemostasis ◽

10.1055/s-0038-1648010 ◽

1976 ◽

Vol 36 (01) ◽

pp. 071-077 ◽

Cited By ~ 2

Author(s):

Daniel E. Whitman ◽

Mary Ellen Switzer ◽

Patrick A. McKee

Keyword(s):

Factor Viii ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

The United States ◽

Fresh Frozen Plasma ◽

Red Cross ◽

Random Samples ◽

Fresh Frozen ◽

Factor Viii Concentrates ◽

Frozen Plasma

SummaryThe availability of factor VIII concentrates is frequently a limitation in the management of classical hemophilia. Such concentrates are prepared from fresh or fresh-frozen plasma. A significant volume of plasma in the United States becomes “indated”, i. e., in contact with red blood cells for 24 hours at 4°, and is therefore not used to prepare factor VIII concentrates. To evaluate this possible resource, partially purified factor VIII was prepared from random samples of fresh-frozen, indated and outdated plasma. The yield of factor VIII protein and procoagulant activity from indated plasma was about the same as that from fresh-frozen plasma. The yield from outdated plasma was substantially less. After further purification, factor VIII from the three sources gave a single subunit band when reduced and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. These results indicate that the approximately 287,000 liters of indated plasma processed annually by the American National Red Cross (ANRC) could be used to prepare factor VIII concentrates of good quality. This resource alone could quadruple the supply of factor VIII available for therapy.

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Low Molecular Weight Trypsin-Plasmin Inhibitors Isolated from Papain Treated Urinary Trypsin Inhibitor

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657115 ◽

1982 ◽

Vol 47 (01) ◽

pp. 014-018 ◽

Cited By ~ 13

Author(s):

H Sumi ◽

N Toki ◽

S Takasugi ◽

S Maehara ◽

M Maruyama ◽

...

Keyword(s):

Trypsin Inhibitor ◽

Gel Electrophoresis ◽

Specific Activity ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Gel Chromatography ◽

Urinary Trypsin Inhibitor ◽

Plasmin Activity ◽

Molecular Weights ◽

Plasmin Inhibitors

SummaryPapain treatment of human urinary trypsin inhibitor (UTI67; mol. wt. 43,000 by SDS-polyacrylamide gel electrophoresis, specific activity 1,897 U/mg protein) produced four new protease inhibitors, which were highly purified by gel chromatography on Sephadex G-100 and isoelectric focusing. The purified inhibitors (UTI26, UTI9-I, UTI9-II, and UTI9-III) were shown to be homogeneous by polyacrylamide disc gel electrophoresis, and had apparent molecular weights of 26,000, 9,000, 9,000, and 9,800, respectively, by sodium dodecyl sulfate gel electrophoresis. During enzymatic degradation of UTI67, the amino acid compositions changed to more basic, and the isoelectric point increased from pH 2.0 (UTI67) to pHs 4.4, 5.2, 6.6, and 8.3 (UTI26, UTI9-I, UTI9-II, and UTI9-III), respectively. Both the parent and degraded inhibitors had anti-plasmin activity as well as antitrypsin and anti-chymotrypsin activities. Much higher anti-plasmin/anti-trypsin and anti-plasmin/anti-chymotrypsin activities were observed in the degraded inhibitors than in the parent UTI67. They competitively inhibited human plasmin with Ki values of 1.13 X 10-7 - 2.12 X 10-6 M (H-D-Val-Leu-Lys-pNA substrate). The reactions were very fast and the active site of the inhibitors to plasmin was thought to be different from that to trypsin or chymotrypsin.

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Identifikasi Daging Tikus Pada Produk Baso Dengan Metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE)

YARSI Medical Journal ◽

10.33476/jky.v26i2.394 ◽

2018 ◽

Vol 26 (2) ◽

pp. 058

Author(s):

Anna P. Roswiem ◽

Triayu Septiani

Keyword(s):

Sodium Dodecyl Sulphate ◽

Gel Electrophoresis ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Polyacrylamide Gel ◽

Sds Page

Bahan baku untuk membuat baso adalah daging hewan, pada umumnya dari daging sapi, ayam, ikan dan babi. Di beberapa daerah di Indonesia terjadi kasus baso tikus. Tujuan penelitian ini adalah menguji ada tidaknya kandungan daging tikus pada produk baso yang dijual di pasar Cempaka Putih-Kecamatan Kramat Jakarta Pusat dan di pedagang baso atau mie baso di sekitar kampus Universitas YARSI Jakarta. Daging adalah protein salah satu metode untuk mengidentifikasi protein adalah metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE). Hasil penelitian menunjukkan bahwa dari 6 sampel baso terindikasi ada 2 sampel baso dengan nomor 1 dan 5 yang dibuat dari campuran daging sapi dan tikus; ada 1 sampel baso dengan nomor 6 yang terbuat dari daging tikus; dan 2 sampel baso dengan nomor 2 dan 3 yang terbuat dari campuran sapi dan babi, dan hanya 1 sampel baso dengan nomor sampel 4 yang benar-benar terbuat dari daging sapi.

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Majra Honey Abrogated the Normal and Cancer Cells Proliferation Inhibition by Juniperus procera Extract and Extract/Honey Generated AgNPs

Anti-Cancer Agents in Medicinal Chemistry ◽

10.2174/1871520620666200213104224 ◽

2020 ◽

Vol 20 (8) ◽

pp. 970-981

Author(s):

Hamed A. Ghramh ◽

Essam H. Ibrahim ◽

Mona Kilnay

Keyword(s):

Anticancer Activity ◽

Cancer Cells ◽

Biological Activities ◽

Sugar Content ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Bioactive Molecules ◽

Sds Page ◽

Splenic Cells ◽

Juniperus Procera

Background: Juniperus procera and Majra honey are well-known as a folk medicine in many countries. Objectives: This work aimed to study the immunomodulatory effects after mixing Majra honey, J. procera water leaves extract and silver Nanoparticles (AgNPs) on immune or cancer cells. Methods: Juniperus procera water leaves extract and 20% Majra honey were prepared. Both the extract and honey were used separately to synthesize AgNPs. AgNPs were characterized using UV/Vis spectrophotometry and electron microscopy. Bioactive molecules in honey and the extract were explored using Fourier Transform Infrared (FT-IR) spectroscopy. Protein profile of honey was explored using Sodium Dodecyl Sulfate- Polyacrylamide Gel Electrophoresis (SDS-PAGE) and honey sugar content was determined using High- Performance Liquid Chromatography (HPLC). Biological activities of honey and the extract were tested. Results: The results demonstrated the ability of the extract/honey to produce AgNPs in a spherical shape. The extract/honey contained many functional groups. SDS-PAGE of Majra honey showed many protein bands. HPLC revealed honey is of good quality and no external additives are added to it. The extract and extract+ AgNPs inhibited the growth of normal rat splenic cells while honey stimulated it. The extract+honey turned stimulatory to the splenic cells’ growth and significantly diminished the inhibitory potential of the extract containing AgNPs. Both the extract and honey have antimicrobial activities, this potential increased in the presence of AgNPs. Honey and Honey+AgNPs inhibited HepG2 cancer cell proliferation while Hela cell growth inhibited only with honey+AgNPs. Conclusion: Both honey and the extract have antibacterial and immunomodulatory potentials as well as the power to produce AgNPs. Majra honey alone showed anticancer activity against HepGe2 cells, but not against Hela cells, and when contained AgNPs had anticancer activity on both cell lines. Mixing of Majra honey with J. procera extract showed characterized immunomodulatory potentials that can be described as immunostimulant.

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