TLS Online TPP Program

#Question id: 14162


A continuous process is set up for treatment of wastewater. Each day, 105 kg cellulose and 103 kg bacteria enter in the feed stream, while 104 kg cellulose and 1.5 x 104 kg bacteria leave in the effluent. The rate of cellulose digestion by the bacteria is 7 x 104 kg d-1. The rate of bacterial growth is 2 x 104 kg d-1 ; the rate of cell death by lysis is 5 x 102 kg d-1. Write balances for cellulose and bacteria in the system.

#SCPH05 I Biotechnology
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TLS Online TPP Program

#Question id: 629

#SCPH05 I Biotechnology

In the presence of a fixed concentration of a competitive inhibitor, which of the following would best characterize an enzyme-catalyzed reaction when the concentration of the substrate is increased?

TLS Online TPP Program

#Question id: 630

#SCPH05 I Biotechnology

In case of competitive inhibition, plots of Km against [Io] fixed [Eo] have

TLS Online TPP Program

#Question id: 631

#SCPH05 I Biotechnology

Two curves showing the rate versus substrate concentration are shown below for an enzyme-catalyzed reaction. One curve is for the reaction in the presence of substance X. The other curve is for data in the absence of substance X. Examine the curves and tell which statement below is false.

TLS Online TPP Program

#Question id: 633

#SCPH05 I Biotechnology

An amino acid transporter protein is responsible for the transport of a specific amino acid across a membrane. The KI values of several competitive inhibitors of the amino acid transporter are shown above. Based on these data, which of the following is most likely the amino acid transported by this protein?

TLS Online TPP Program

#Question id: 634

#SCPH05 I Biotechnology

An enzyme has a Vmax of 50 micromol product formed (minute x mg protein)-1 and a Km of 10 microM for the substrate. When a reaction mixture contains the enzyme and 5 microM substrate, which of the following percentages of the maximum velocity will be closest to the initial reaction rate?

TLS Online TPP Program

#Question id: 635

#SCPH05 I Biotechnology

The enymatic rate constant (kcat/Km) of orotidine 5ʹ-phosphate decarboxylase is 6 x 107 M-1s-1 and the nonenzymatic rate constant (kn) is 3 x 10-16 s-1.  What is the value of the enzymeʹs catalytic proficiency?