A fermentation slurry containing Streptomyces kanamyceticus cells is filtered using a continuous rotary vacuum filter. 120 kg h^{- 1} slurry is fed to the filter; 1 kg slurry contains 60 g cell solids. To improve filtration rates, particles of diatomaceous-earth filter aid are added at a rate of 10 kg h^{- 1}. The concentration of kanamycin in the slurry is 0.05% by weight. Liquid filtrate is collected at a rate of 112 kg h^-1; the concentration of kanamycin in the filtrate is 0.045% (w/w). Filter cake containing cells and filter aid is continuously removed from the filter cloth.

 What percentage liquid is the filter cake?

#Question id: 561

#SCPH05 I Biotechnology

Enzyme X exhibits maximum activity at pH = 6.9.  X shows a fairly sharp decrease in its activity when the pH goes much lower than 6.4.  One likely interpretation of this pH activity is that:

#Question id: 561

#SCPH06 I Botany

Enzyme X exhibits maximum activity at pH = 6.9.  X shows a fairly sharp decrease in its activity when the pH goes much lower than 6.4.  One likely interpretation of this pH activity is that:

#Question id: 561

#SCPH28 | Zoology

Enzyme X exhibits maximum activity at pH = 6.9.  X shows a fairly sharp decrease in its activity when the pH goes much lower than 6.4.  One likely interpretation of this pH activity is that:

#Question id: 562

#SCPH01 Biochemistry

Phenyl-methane-sulfonyl-fluoride (PMSF) inactivates serine proteases by binding covalently to the catalytic serine residue at the active site; this enzyme-inhibitor bond is not cleaved by the enzyme.  This is an example of what kind of inhibition?

#Question id: 562

#I Life Science/ Life Sciences Group – I-V

Phenyl-methane-sulfonyl-fluoride (PMSF) inactivates serine proteases by binding covalently to the catalytic serine residue at the active site; this enzyme-inhibitor bond is not cleaved by the enzyme.  This is an example of what kind of inhibition?

#Question id: 562

#SCPH05 I Biotechnology

Phenyl-methane-sulfonyl-fluoride (PMSF) inactivates serine proteases by binding covalently to the catalytic serine residue at the active site; this enzyme-inhibitor bond is not cleaved by the enzyme.  This is an example of what kind of inhibition?