Answer:
12.44 g
Explanation:
2C4H10 + 13O2 = 8CO2 + 10H2O
n(C4H10) = m(C4H10)/M(C4H10) = 4.1 / 58g/mol = 0.0707 mol (excess).
n(O2) = m(O2)/M(O2) = 25.9 / 32g/mol = 0.809 mol (deficiency).
Since the ratio of O2 to octane is 13 : 2 we can divide 0.0707 by 2 to get 0.03535 and divide 0.809 by 13 to get 0.062.
mass of CO2 produced =
M = [0.0707 moles C4H10 x 8 moles CO2] / 2 moles C4H10 x 44 g CO2/mol
M = 0.5656/2 * 44
M = 0.2828 * 44
M = 12.44 of CO2
The equation of 5m+4=7m+6 is equal to m=-1
I think its C: due to mixing and oceanic.....
Answer:The lone pair of electrons takes up more space than a regular bonding pair since it it is not confined to be between two atoms, so it adds coulombic repulsion to the bonding pairs and compresses the angle. Therefore, the bond angle is less than the standard 109.5∘ . It is actually 97.7∘
The production of manganese peroxidase (MnP) by Irpex lacteus, purified to electrophoretic homogeneity by acetone precipitation, HiPrep Q and HiPrep Sephacryl S-200 chromatography, was shown to correlate with the decolorization of textile industry wastewater. The MnP was purified 11.0-fold, with an overall yield of 24.3%. The molecular mass of the native enzyme, as determined by gel filtration chromatography, was about 53 kDa. The enzyme was shown to have a molecular mass of 53.2 and 38.3 kDa on SDS-PAGE and MALDI-TOF mass spectrometry, respectively, and an isoelectric point of about 3.7. The enzyme was optimally active at pH 6.0 and between 30 and 40 degrees C. The enzyme efficiently catalyzed the decolorization of various artificial dyes and oxidized Mn (II) to Mn (III) in the presence of H(2)O(2). The absorption spectrum of the enzyme exhibited maxima at 407, 500, and 640 nm. The amino acid sequence of the three tryptic peptides was analyzed by ESI Q-TOF MS/MS spectrometry, and showed low similarity to those of the extracellular peroxidases of other white-rot basidiomycetes.
