The described system is designed to measure the field map of pulse bending magnets of accelerators. As an example, the magnet, which is an element of the particle bypass channel from the booster to ...the nuclotron of the NICA complex, which is being created at JINR, is chosen. Analyzing the capabilities of various methods in pulsed-field measurements and requirements for measurement errors in bending magnets better than 10
–3
have led to the development of a method based on the use of Hall probes. The article substantiates the developed method, describes its capabilities, and the hardware developed for conducting measurements. In the conclusions, results of measurements of pulsed bending magnets of the booster–nuclotron channel are presented and analyzed.
A method proposed to preserve the electron beam polarization at the VEPP-4M collider during acceleration with crossing the integer (imperfection) spin resonance at energyE=1763MeVhas been ...successfully applied. It is based on full decompensation of the0.6×3.3Tesla×meterintegral of the KEDR detector longitudinal magnetic field due to the antisolenoid being “switched off.”
Using chromatography on different matrixes, three β-glucosidases (120, 116, and 70 kDa) were isolated from enzymatic complexes of the mycelial fungi Aspergillus japonicus, Penicillium verruculosum, ...and Trichoderma reesei, respectively. The enzymes were identified by MALDI-TOF mass-spectrometry. Substrate specificity, kinetic parameters for hydrolysis of specific substrates, ability to catalyze the transglucosidation reaction, dependence of the enzymatic activity on pH and temperature, stability of the enzymes at different temperatures, adsorption ability on insoluble cellulose, and the influence of glucose on catalytic properties of the enzymes were investigated. According to the substrate specificity, the enzymes were shown to belong to two groups: i) β-glucosidase of A. japonicus exhibiting high specific activity to the low molecular weight substrates cellobiose and pNPG (the specific activity towards cellobiose was higher than towards pNPG) and low activity towards polysaccharide substrates (β-glucan from barley and laminarin); ii) β-glucosidases from P. verruculosum and T. reesei exhibiting relatively high activity to polysaccharide substrates and lower activity to low molecular weight substrates (activity to cellobiose was lower than to pNPG).
The effect of polysaccharide monooxygenase (endoglucanase IV) from the fungus Trichoderma reesei on the hydrolysis of polysaccharide substrates by cellulases secreted by the fungus Penicillium ...verruculosum has been investigated. Supplementation of the enzyme complex from P. verruculosum by endoglucanase IV from T. reesei has been shown to elevate the efficiency of cellulose hydrolysis by 45%.
Methods for the production and analysis of cellulase and hemicellulase enzyme preparations of various compositions based on the Penicillium verruculosum carbohydrase complex and intended for the ...effective hydrolysis of different types of cellulose-containing materials (CCMs) have been developed. New recombinant strains of P. verruculosum producing multienzyme carbohydrase complexes with increased activities of cellulases (due to the expression of endo-β-1,4-glucanases I and IV and cellobiohydrolase II from Trichoderma reesei) and hemicellulases (due to the expression of endo-β-1,4-xylanases from P. canescens and T. reesei and endo-β-1,4-mannanase from T. reesei) were constructed. The hydrolytic efficiency of the enzyme preparations (EPs) produced by the new recombinant strains during continuous hydrolysis of three CCM types (milled aspen, depitched pine wood, and milled bagasse) was studied. It was shown that new EPs containing recombinant proteins and retaining their own basic cellulase complex are characterized by the highest hydrolytic ability, exceeding that of the EP based on the original P. verruculosum strain. The recombinant enzyme preparations were highly stable; the optimal pH and temperature values for cellulase, xylanase and mannanase activities were in the range of 3.5–5.5 and 50–80°C, respectively.
The genes
inuA
and
inu1
, encoding two inulinases (32nd glycosyl hydrolase family) from filamentous fungi
Aspergillus niger
and
A. awamori
, were cloned into
Penicillium canescens
recombinant strain. ...Using chromatographic techniques, endoinulinase InuA (56 kDa, p
I
3) and exoinulinase Inu1 (60 kDa, p
I
4.3) were purified to homogeneity from the enzymatic complexes of
P. canescens
new transformants. The properties, such as substrate specificity, pH- and T-optima of activity, stability at different temperatures, influence of cations and anions on the catalytic activity, etc., of both recombinant inulinases were studied.
We present the first accurate results of measurements of the tensor analyzing power component
T
20
for the coherent neutral pion photoproduction on the deuteron. The measurements were performed at ...the Budker Institute of Nuclear Physics at VEPP-3 storage ring using the internal tensor polarized deuterium target. The measurements cover the region of photon energy from 200 to 450 MeV and the region of the center-of-mass pion polar angle from 100 to 140 degrees. The results obtained are compared with predictions of several theoretical models.
We present experimental results for T20 component of the tensor analyzing power for incoherent π− photoproduction on a deuteron. The experiment was performed on an internal tensor-polarized gas ...deuterium target of the VEPP-3 electron storage ring in 2021 using the proton-proton coincidence method. The data are compared with the results of numerical simulation.
An enzyme preparation has been produced on the basis of Penicillium canescens strains with the activity of cellibiohydrolase I, II; endo-1,4-β-gluconase of Penicillium verruculosum; and β-glucosidase ...of Aspergillus niger. It was shown that for the most effective hydrolysis of aspen wood pulp the optimal ratio of cellobiohydrolase and endo-1,4-β-gluconase in enzyme preparations was 8: 2 (by protein). It was also established that the homologous xylanase secreted by the Penicillium canescens fungus is a required component for the enzyme complex for hydrolysis of the hemicellulose matrix of aspen wood.
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