Electrical<span> energy is produced by dry cell. Hope that helps.</span>
Answer:
Attached below
Explanation:
Free energy of mixing = ΔGmix = Gf - Gi
attached below is the required derivation of the
<u>a) Molar Gibbs energy of mixing</u>
ΔGmix = Gf - Gi
hence : ΔGmix = ∩RT ( X1 In X1 + X2 In X2 + X3 In X3 + ------- )
<u>b) molar excess Gibbs energy of mixing</u>
Ni = chemical potential of gas
fi = Fugacity
N°i = Chemical potential of gas when Fugacity = 1
ΔG = RT In ( a2 / a1 )
<em>V = 151 mL = 151 cm³</em>
<em>d = 0,789 g/mL = 0,789 g/cm³</em>
--------------------------------------
d = m/V
m = d×V
m = 0,789×151
<u>m = 119,139g</u>
Answer : 
is the molecule that exhibit dipole-dipole forces as its strongest intermolecular force.
Explanation : The shape or geometry of given molecules of 
, 
, 
, 
and are linear, linear, tetrahedral, trigonal planar and angular respectively.
The given molecules , , , are symmetrical molecules. These symmetric molecules cannot exists as dipole even they contain polar bonds. Thus, these molecules will not exhibit dipole-dipole forces.
molecule has polar bonds and unsymmetrical bonds as shown in attached image. This molecule cannot exhibit H-bonding. It exhibit only dipole-dipole forces.
Therefore, molecule exhibit dipole-dipole forces as strongest intermolecular force.
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.
