scholarly journals Quality, Microstructure, and Technological Properties ofSheepMeat Marinated in Three Different Ways

2017 ◽  
Vol 2017 ◽  
pp. 1-10
Author(s):  
Dessislava Borislavova Vlahova-Vangelova ◽  
Stefan Georgiev Dragoev ◽  
Dessislav Kostadinov Balev ◽  
Bahytkul Kajkenovna Assenova ◽  
Kumarbek Junusbekovich Amirhanov
Keyword(s):  
Protein Solubility ◽  
Amino Nitrogen ◽  
Sodium Lactate ◽  
Technological Properties ◽  
Lipid Fractions ◽  
Sds Page ◽  
Lipid And Protein Oxidation ◽  
Oil Emulsions ◽  
Prooxidant Action ◽  
Page Electrophoresis

The objective of this study was to explore the effect of 24 and 48 h alkaline (2% pentasodium tripolyphosphate), acid (2% sodium lactate), and water-oil marinating (water : sun flavor oil = 1 : 1 and 2% salt) as well as brine soaking (2% salt) on microstructure, changes in protein, and lipid fractions and technological properties of sheep (m. Longissimus dorsi). Strong myofibrillar fragmentation after 48 h alkaline marinating was observed. Significant swelling and increasing of spaces between myofibrils were found after 24 h brine soaking. Marinating in water-oil emulsions did not show a significant impact on the muscle microstructure. Alkaline and acid marinating as well as salt soaking promote the myofibrillar protein solubility and increased the free amino nitrogen content. After 24 h acid and 48 h alkaline marinating SDS-PAGE electrophoresis showed increasing of 25–30 kDa protein bands. The results obtained for the lipid and protein oxidation confirm prooxidant action of the sodium lactate (2%) and antioxidant effect of polyphosphates (2%) in marinated sheep.

scholarly journals Study of the proteins in the defatted flour and protein concentrate of baru nuts (Dipteryx alata Vog)

2012 ◽  
Vol 32 (3) ◽  
pp. 464-470 ◽  
Author(s):  
Rita de Cássia Avellaneda Guimarães ◽  
Simone Palma Favaro ◽  
Antonio Camilo Arguelho Viana ◽  
José Antônio Braga Neto ◽  
Valdir Augusto Neves ◽  
...  
Keyword(s):  
Functional Properties ◽  
Protein Solubility ◽  
Absorption Capacity ◽  
In Vitro Digestibility ◽  
Protein Concentrate ◽  
Emulsifying Properties ◽  
Lipid Fractions ◽  
Sds Page ◽  
Dipteryx Alata

Baru (Dipteryx alata Vog.) is an abundant legume in the Brazilian Savanna. Its nuts can be exploited sustainably using its protein and lipid fractions. This study aimed to analyze the proteins of the nuts present in the defatted flour and protein concentrate in terms of their functional properties, the profile of their fractions, and the in vitro digestibility. The flour was defatted with hexane and extracted at the pH of higher protein solubility to obtain the protein concentrate. The electrophoretic profile of the protein fractions was evaluated in SDS-PAGE gel. The functional properties of the proteins indicate the possibility of their use in various foods, like soybeans providing water absorption capacity, oil absorption capacity, emulsifying properties, and foamability. Globulins, followed by the albumins, are the major fractions of the flour and protein concentrate, respectively. Digestibility was greater for the concentrate than for the defatted flour.

scholarly journals Establishment of peritoneal liquid electrophoretogram from healthy horses and horses submitted to experimentally induced intestinal obstruction

2014 ◽  
Vol 66 (3) ◽  
pp. 665-671 ◽  
Author(s):  
A.F.S. Nogueira ◽  
P.A. Di Filippo ◽  
L.A. Anai ◽  
M.C. Vieira ◽  
K.M.M.G. Simplício ◽  
...  
Keyword(s):  
Intestinal Obstruction ◽  
Acute Phase ◽  
Acute Phase Proteins ◽  
Immunoglobulin A ◽  
Control Group ◽  
Protein Levels ◽  
Sds Page ◽  
Significant Difference ◽  
Page Electrophoresis ◽  
Experimentally Induced

The initial inflammatory stages of the colic syndrome include changes known as acute phase response. The aim of this study was to contribute with the establishment of reference values concerning the electrophoretogram of peritoneal liquid from healthy horses and horses submitted to experimentally induced intestinal obstruction. Twenty-one horses were allotted in four groups: duodenal obstruction (DG), ileum obstruction (IG), left-dorsal colon obstruction (MG), and control group (CG). Peritoneal liquid was sampled before obtruction (T0), with 3 hours of obstruction (T3) and 6, 30, 102 and 174 hours after desobstructing (T6, T30, T102 and T174, respectively). Total protein levels were determined by the biuret method and protein fractions were obtained by SDS-PAGE electrophoresis. The acute phase proteins (APP) identified were Immunoglobulin-A, ceruloplasmin, transferrin, albumin, α1-antitrypsin, heavy and light chains of immunoglobulin-G, haptoglobin, α1-acid glycoprotein and a still unnamed protein, which was called P24. There was no difference (P>0.3) in protein levels among groups, although a significant difference (P>0.05) was observed between distinct experimental moments in each group evidencing a higher response of the APP in the obstructed groups. The APP fractioning of the peritoneal liquid was standardized to establish a standard curve for healthy equines and those submitted to induced intestinal obstruction. Moreover, it was verified that the SDS-PAGE electrophoresis was sensitive and effective to help diagnose abdominal inflammatory processes.

scholarly journals Royal Jelly and Its SDS-PAGE Electrophoresis Profiles

2019 ◽  
pp. 17-20
Author(s):  
Hilal Ebru Çakır ◽  
Yakup Şirin ◽  
Sevgi Kolaylı
Keyword(s):  
Royal Jelly ◽  
Sds Page ◽  
Page Electrophoresis

scholarly journals Coal Depolymerising Activity and Haloperoxidase Activity of Mn Peroxidase fromFomes durissimusMTCC-1173

2011 ◽  
Vol 2011 ◽  
pp. 1-8 ◽  
Author(s):  
Sunil Kumar Singh ◽  
Meera Yadav ◽  
Sudha Yadava ◽  
Kapil Deo Singh Yadav
Keyword(s):  
Deae Cellulose ◽  
Anion Exchange Chromatography ◽  
Sodium Lactate ◽  
Low Ph ◽  
Exchange Chromatography ◽  
Fungal Strain ◽  
Mn Peroxidase ◽  
Sds Page ◽  
Catalytic Rate ◽  
Temperature Optima

Mn peroxidase has been purified to homogeneity from the culture filtrate of a new fungal strainFomes durissimusMTCC-1173 using concentration by ultrafiltration and anion exchange chromatography on diethylaminoethyl (DEAE) cellulose. The molecular mass of the purified enzyme has been found to be 42.0 kDa using SDS-PAGE analysis. The values using MnSO4and H2O2as the variable substrates in 50 mM lactic acid-sodium lactate buffer pH 4.5 at were 59 μM and 32 μM, respectively. The catalytic rate constants using MnSO4and H2O2were 22.4 s−1and 14.0 s−1, respectively, giving the values of 0.38 μM−1s−1and 0.44 μM−1s−1, respectively. The pH and temperature optima of the Mn peroxidase were 4 and , respectively. The purified MnP depolymerises humic acid in presence of H2O2. The purified Mn peroxidase exhibits haloperoxidase activity at low pH.

scholarly journals Evaluation of NaCl and KCl Salting Effects on Technological Properties of Pre- and Post-Rigor Chicken Breasts at Various Ionic Strengths

Foods ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 721
Author(s):  
Dong-Heon Song ◽  
Youn-Kyung Ham ◽  
Sin-Woo Noh ◽  
Koo Bok Chin ◽  
Hyun-Wook Kim
Keyword(s):  
Ionic Strength ◽  
Ph Value ◽  
Protein Solubility ◽  
Textural Properties ◽  
Myofibrillar Protein ◽  
Cooking Loss ◽  
Technological Properties ◽  
Raw Meat

The objective of this study is to evaluate the effects of NaCl and KCl salting on technological properties of pre- and post-rigor chicken breasts at various ionic strengths. The following factorial arrangement was used: 2 salt types (NaCl and KCl) × 2 rigor statuses (pre- and post-rigor) × 4 ionic strengths (0.086, 0.171, 0.257, and 0.342). Hot-boned and ground chicken breasts were salted within 30 min postmortem after slaughter (pre-rigor salting) or 24 h postmortem (post-rigor salting) with varying concentrations of NaCl (0.50%, 1.00%, 1.50%, and 2.00%) or KCl (0.64%, 1.28%, 1.91%, and 2.55%) corresponding to the four ionic strengths. KCl caused higher pH value in salted chicken breasts than NaCl (p < 0.05). However, KCl decreased total and myofibrillar protein solubilities in post-rigor salted chicken breasts compared to NaCl (p < 0.05), but those were similar to pre-rigor chicken breasts, regardless of the salt type (p > 0.05). Different salt types had no significant impact on cooking loss and textural properties. This study shows that NaCl and KCl had similar effects on technological properties at the same ionic strength (within 0.342), but the use of KCl may have the possibility to decrease protein solubility, depending on rigor status of raw meat at the different salting time.

scholarly journals Growth characteristics and dynamics of protein synthesis in callus cultures from Glycine wightii (Wight & Arn.) Verdc.

2005 ◽  
Vol 29 (6) ◽  
pp. 1161-1166 ◽  
Author(s):  
André Luis Coelho da Silva ◽  
Cecília Sulzbacher Caruso ◽  
Renato de Azevedo Moreira ◽  
Ana Cecília Góes Horta
Keyword(s):  
Protein Synthesis ◽  
Growth Curve ◽  
Dry Weight ◽  
Callus Cultures ◽  
Exponential Phase ◽  
Cotyledon Explants ◽  
Ph Values ◽  
Freeze Dried ◽  
Sds Page ◽  
Page Electrophoresis

Cotyledon explants were first cultured on MS medium supplemented with 4.52 M 2,4-D and 0.46 mM kinetin. The development of the calli was followed (0, 4, 8, 12, 16, 20, 24, 28 and 32 days after) and the growth curve was determined, based in fresh and dry weight. The growth curve presented sigmoidal form with four distinct phases. The highest growth percentage was observed at the exponential phase and the lowest at the stationary phase. These results indicated that cotyledon callus subculture should be performed 20 days after inoculation. The calli obtained after a period of 28 days were freeze dried, macerated and submitted to extraction with buffers of different pH values (2.6; 4.0; 6.0; 8.0 and 10.0) and the proteins in the extracts were determined by Bradford method. The pH 8.0 buffer was the most efficient to extract the largest amount of protein. The amino acid analyses calli showed a high content of aspartic acid and low content of metionin. The dynamics of protein synthesis in calli was followed by SDS-PAGE electrophoresis.

scholarly journals Enhanced Solubility of Rapeseed Meal Protein Isolates Prepared by Sequential Isoelectric Precipitation

Foods ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 703
Author(s):  
Hristo Kalaydzhiev ◽  
Radoslav Georgiev ◽  
Petya Ivanova ◽  
Magdalena Stoyanova ◽  
Cristina L. M. Silva ◽  
...  
Keyword(s):  
Protein Solubility ◽  
Rapeseed Meal ◽  
Protein Isolate ◽  
Protein Fractions ◽  
Isoelectric Precipitation ◽  
Protein Isolates ◽  
Sds Page ◽  
Enhanced Solubility ◽  
Meal Protein ◽  
Biochemical Analyses

The solubility of plant protein isolates is a key determinant of their potential application. Two protein isolates (PI) from ethanol-treated industrial rapeseed meal, PI10.5–2.5 and PI2.5–8.5, were prepared by sequential isoelectric precipitation of alkali-extracted proteins (pH 12) starting from pH 10.5 to 2.5 or from pH 2.5 to 8.5, respectively. Biochemical analyses revealed that PI2.5–8.5 contained a higher amount of crude protein (72.84%) than PI10.5–2.5 (68.67%). In the same protein isolate, the level of total phenols (0.71%) was almost two-fold higher than that in PI10.5–2.5 (0.42%). No glucosinolates were established in both protein isolates. SDS-PAGE analysis demonstrated that PI10.5–2.5 contained 10 to 15 kDa protein fractions in a relatively higher amount, while PI2.5–8.5 was enriched in 18 to 29 kDa protein fractions. PI10.5–2.5 exhibited high solubility, varying from 41.74% at pH 4.5 to 65.13% at pH 6.5, while PI2.5–8.5 was almost two-fold less soluble under the same conditions. Up to pH 5.5, the addition of NaCl at 0.03 and 0.25 M diminished the solubility of PI2.5–8.5, while the solubility of PI10.5–2.5 was increased. The supplementation of PI10.5–2.5 with 0.25 M NaCl enhanced the protein solubility to 56.11% at pH 4.5 and 94.26% at pH 6.5. The addition of 0.03 M NaCl also increased the solubility of this protein isolate but to a lower extent. Overall, the approach for sequential precipitation of proteins influenced the biochemical characteristics, protein fractional profile and solubility of prepared protein isolates.

scholarly journals Characterization and purification of a novel dATP-binding protein in eukaryotes

1992 ◽  
Vol 287 (3) ◽  
pp. 871-879 ◽  
Author(s):  
A Dalton ◽  
D P Hornby ◽  
S P Langston ◽  
G M Blackburn
Keyword(s):  
Binding Protein ◽  
Active Form ◽  
Direct Interaction ◽  
Nuclear Fraction ◽  
Yeast Saccharomyces Cerevisiae ◽  
Naturally Occurring ◽  
Sds Page ◽  
Marked Preference ◽  
High Degree ◽  
Page Electrophoresis

We characterized and purified an acidic dATP-binding protein, which, in its active form, resides in the nuclear fraction of a range of cells from mammals (including pig liver) and baker's yeast (Saccharomyces cerevisiae). This protein exhibits a high degree of specificity for the deoxy form of the naturally occurring nucleoside triphosphates and shows a marked preference for the purine deoxynucleoside triphosphates dATP and dGTP. The protein cleaves the terminal phosphate of dATP and appears to retain the dADP moiety of the nucleotide in a reaction that is resistant to both SDS and 8 M-urea. Fractionation of the nuclear preparation followed by non-denaturing PAGE and SDS/PAGE electrophoresis was sufficient to produce pure protein. The occurrence of this activity in all nuclei tested suggests that it plays an important role in nuclear metabolism. The specificity of the enzyme for deoxynucleoside triphosphates further suggests a role for this enzyme in DNA replication or repair, but the acidity of the protein argues against a direct interaction with DNA, and, indeed, the catalytic activity is not modulated by the inclusion of DNA in a variety of physical forms.

Sign in / Sign up

Export Citation Format

Share Document