scholarly journals Compatibility and Washing Performance of Compound Protease Detergent

2021 ◽  
Vol 12 (1) ◽  
pp. 150
Author(s):  
Wei Zhang ◽  
Jintao Wu ◽  
Jing Xiao ◽  
Mingyao Zhu ◽  
Haichuan Yang
Keyword(s):  
Molecular Weight ◽  
Fourier Transform ◽  
Photoelectron Spectroscopy ◽  
Gel Electrophoresis ◽  
Enzyme Preparation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Cost Effective ◽  
Water Softening ◽  
X Ray ◽  
Before And After

Protease is the main enzyme of detergent. Through the combination of different proteases and the combination of protease and detergent additives, it can adapt to different washing conditions to improve the washing effect. In this experiment, whiteness determination, microscope scanning, Fourier transform infrared spectroscopy, and X-ray photoelectron spectroscopy were used to detect the whiteness values of the cloth pieces before and after washing, as well as the stain residue between the fibers on the surface of the cloth pieces. The protease detergent formula with better decontamination and anti-deposition effects was selected. The combination of alkaline protease, keratinase, and trypsin was cost-effective in removing stains. Polyacrylamide gel electrophoresis showed that the molecular weight of the protein significantly changed after adding the enzyme preparation during washing, and the molecular weight of the protein was directly proportional to protein redeposition. The composite protease had a better comprehensive decontamination effect, and when compatible with suitable surfactants, anti-redeposition agents, and water-softening agents, the compound protease detergent exhibited a stronger decontamination ability than commercial detergents.

scholarly journals Synthesis of Novel Arginine-Based Flame Retardant and Its Application in Lyocell Fabric

Molecules ◽  
2021 ◽  
Vol 26 (12) ◽  
pp. 3588
Author(s):  
Jiayi Chen ◽  
Yansong Liu ◽  
Jiayue Zhang ◽  
Yuanlin Ren ◽  
Xiaohui Liu
Keyword(s):  
Fourier Transform ◽  
Heat Release ◽  
Flame Retardant ◽  
Photoelectron Spectroscopy ◽  
Fourier Transform Infrared ◽  
Ftir Analysis ◽  
Excellent Thermal Stability ◽  
X Ray ◽  
Cone Calorimeter Test ◽  
Before And After

Lyocell fabrics are widely applied in textiles, however, its high flammability increases the risk of fire. Therefore, to resolve the issue, a novel biomass-based flame retardant with phosphorus and nitrogen elements was designed and synthesized by the reaction of arginine with phosphoric acid and urea. It was then grafted onto the lyocell fabric by a dip-dry-cure technique to prepare durable flame-retardant lyocell fabric (FR-lyocell). X-ray photoelectron spectroscopy (XPS) and Fourier-transform infrared spectroscopy (FTIR) analysis demonstrated that the flame retardant was successfully introduced into the lyocell sample. Thermogravimetric (TG) and Raman analyses confirmed that the modified lyocell fabric featured excellent thermal stability and significantly increased char residue. Vertical combustion results indicated that FR-lyocell before and after washing formed a complete and dense char layer. Thermogravimetric Fourier-transform infrared (TG-FTIR) analysis suggested that incombustible substances (such as H2O and CO2) were produced and played a significant fire retarding role in the gas phase. The cone calorimeter test corroborated that the peak of heat release rate (PHRR) and total heat release (THR) declined by 89.4% and 56.4%, respectively. These results indicated that the flame retardancy of the lyocell fabric was observably ameliorated.

Extracellular endodextranase from the yeast Lipomyces starkeyi

1983 ◽  
Vol 29 (9) ◽  
pp. 1092-1095 ◽  
Author(s):  
E. Webb ◽  
I. Spencer-Martins
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Minimal Medium ◽  
Enzyme Preparation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Extracellular Fluid ◽  
Sole Source ◽  
Optimum Temperature ◽  
Lipomyces Starkeyi ◽  
High Concentrations

Strain IGC 4047 of the yeast Lipomyces starkeyi grew well with dextran as sole source of carbon and energy, and was able to hydrolyse blue dextran and Sephadex G-100. The enzyme was partially purified by fractionated isopropanol precipitation from the extracellular fluid of cultures grown in a minimal medium with dextran. The enzyme preparation showed only one band by polyacrylamide gel electrophoresis. The enzyme had the following properties: molecular weight, 23 000; optimum temperature and pH for activity, around 50 °C and pH 5.0, respectively; pH stability, pH 3.5–7.5; after 2 h at 50 °C and pH 5.0, 30% reduction in activity; isoelectric point, pI = 5.4; final products of dextran hydrolysis, isomaltooligosaccharides from glucose up to isomaltohexaose, with high concentrations of isomaltose and isomaltotriose. These results suggest that the enzyme is an endodextranase.

Effects of Thrombin, Chymotrypsin and Aggregated Gamma-Globulins on the Proteins of the Human Platelet Membrane

1977 ◽  
Vol 37 (03) ◽  
pp. 396-406 ◽  
Author(s):  
B Podolsak
Keyword(s):  
Molecular Weight ◽  
Platelet Activation ◽  
Gel Electrophoresis ◽  
Human Platelet ◽  
Polyacrylamide Gel Electrophoresis ◽  
Platelet Membrane ◽  
Low Molecular Weight ◽  
Membrane Glycoproteins ◽  
Membrane Component ◽  
Before And After

SummaryAnalysis of platelet membrane proteins and glycoproteins by SDS Polyacrylamide gel electrophoresis was carried out before and after treatment with thrombin. Extended incubation with thrombin (in the presence of EDTA or adenosine, which inhibit aggregation) produced extensive changes in the bands observed. With incubation times of a few minutes however, the changes were restricted to a glycopeptide, GP IV (approx. 90,000 Daltons) and one or two polypeptides of low molecular weight, in particular polypeptide 16 (approx. 23,000 Daltons). At 0–3° C only polypeptide 16 was still hydrolyzed.Chymotrypsin, which does not activate platelets, attacked glycopeptides I, II, III but no changes were apparent in GP IV and polypeptide 16. When chymotrypsin-treated platelets were further incubated with thrombin, only GP IV and one to two low molecular weight polypeptides, especially polypeptide 16, were affected. As polypeptide 16 appears to be an integral membrane component it is possible that it, either by itself or in combination with GP IV, represents the primary thrombin substrate involved in platelet activation.Aggregated IgG, which also activates platelets, does not modify the membrane glycoproteins but does change the low molecular weight region in particular band 16.

scholarly journals Oxidative Depression of Arsenopyrite by Using Calcium Hypochlorite and Sodium Humate

Minerals ◽  
2018 ◽  
Vol 8 (10) ◽  
pp. 463 ◽  
Author(s):  
Shangyong Lin ◽  
Runqing Liu ◽  
Yongjie Bu ◽  
Chen Wang ◽  
Li Wang ◽  
...  
Keyword(s):  
Fourier Transform ◽  
Photoelectron Spectroscopy ◽  
Cost Effective ◽  
Arsenic Content ◽  
Mineral Surfaces ◽  
Calcium Hypochlorite ◽  
X Ray ◽  
Sodium Humate ◽  
Environmental Friendly ◽  
Mineral Flotation

During smelting, arsenic in copper concentrates affects the product quality and causes environmental pollution. Removing arsenic minerals from copper concentrates requires environmental-friendly and cost-effective depressants for flotation separation. Ca(ClO)2 was combined with sodium humate (SH) to improve the flotation separation of chalcopyrite from arsenopyrite. Results of single-mineral flotation indicated that combined Ca(ClO)2 and SH significantly inhibited arsenopyrite and exerted a negligible effect on chalcopyrite. The arsenic content in copper concentrates significantly decreased from 63% to 11% in the absence of a depressant and in the presence of Ca(ClO)2 and SH, as proven by the mixed-mineral flotation results. SH can adsorb on both mineral surfaces as indicated by the zeta potential measurements and Fourier transform infrared spectroscopy. However, the presence of Ca(ClO)2 increased the adsorption of arsenopyrite compared with chalcopyrite. The arsenopyrite floatability depressed with the Ca(ClO)2 oxidation and subsequent SH adsorption, as verified by X-ray photoelectron spectroscopy. Results of flotation tests confirmed that the chalcopyrite surface was slightly oxidized, but it remained hydrophobic. The combination of depressants has the potential for industrial application.

Purification of 7α-hydroxysteroid dehydrogenase from Escherichia coli strain 080

1990 ◽  
Vol 36 (2) ◽  
pp. 131-135 ◽  
Author(s):  
Vijay Prabha ◽  
Meenakshi Gupta ◽  
D. Seiffge ◽  
K. G. Gupta
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Key Words ◽  
Ammonium Sulfate ◽  
Gel Electrophoresis ◽  
Enzyme Preparation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Deae Cellulose ◽  
Hydroxysteroid Dehydrogenase ◽  
Coli Strain

Purification studies of 7α-hydroxysteroid dehydrogenase (7α-HSDH) (EC 1.1.1.159) from Escherichia coli 080 showed that 1.59-fold purification could be achieved by heating (60 °C for 10 min) the ultracentrifuged enzyme preparation, and 6.46-fold purification was achieved by subsequent precipitation with ammonium sulfate. Further purification on Sephadex G-100 gel gave 10.1-fold purification. After pooling and concentrating the active fractions obtained from the Sephadex G-100 filtration, an 11.1-fold purification was achieved using DEAE-cellulose chromatography. The purified enzyme produced a single band on polyacrylamide gel electrophoresis and its molecular weight was determined to be 54 000. The enzyme was immunogenic and showed immunoprecipitation with homologus antisera. Key words: 7α-hydroxysteroid dehydrogenase, Escherichia coli.

Mechano-Chemical Modification of Nanodiamond with GW

2008 ◽  
Vol 375-376 ◽  
pp. 87-91
Author(s):  
Yong Wei Zhu ◽  
Xiang Yang Xu ◽  
Bai Chun Wang ◽  
Jian Liang Shen
Keyword(s):  
Fourier Transform ◽  
Chemical Modification ◽  
Photoelectron Spectroscopy ◽  
Silane Coupling Agent ◽  
Xps Spectra ◽  
X Ray ◽  
Silane Coupling ◽  
Before And After ◽  
New Type ◽  
Ft Ir

Mechano-chemical modification (MCM) of nanodiamond was conducted with a stirring mill. A new type of silane coupling agent, GW was chosen as its modifier. X-ray photoelectron spectroscopy (XPS) and Fourier transform infrared (FT-IR) were employed to study the surface properties of nanodiamond before and after treatments. Results showed that the peaks related to GW and the ball (for example, Fe, Si and Cl) appeared obviously after its MCM on their XPS spectra and mostly disappeared after its further purification with acid X or Y. A new peak located at 1382.48cm-1 was very strong after further purification. It was proven by their FT-IR spectra.

scholarly journals An improved procedure for the isolation of 3-phosphoglycerate kinase from yeast

1971 ◽  
Vol 122 (1) ◽  
pp. 89-92 ◽  
Author(s):  
R. K. Scopes
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Phosphoglycerate Kinase ◽  
X Ray Diffraction ◽  
X Ray ◽  
Starch Gel ◽  
Crystalline Forms

3-Phosphoglycerate kinase has been isolated from yeast by a new procedure. Over 1g was obtained from 450g of granulated baker's yeast; it had a specific activity of up to 940units/mg at 30°C. Six distinct crystalline forms have been grown, at least one of these being suitable for X-ray diffraction studies. The crystalline preparation is pure, judged by starch-gel or sodium dodecyl sulphate–polyacrylamide-gel electrophoresis; the latter method indicating that the enzyme is monomeric, with a molecular weight near to 50000.

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

1992 ◽  
Vol 68 (05) ◽  
pp. 534-538 ◽  
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).

Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.

Sign in / Sign up

Export Citation Format

Share Document