Which condition favors the bond formation______

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#Question id: 14363

#Section 5: Bioprocess Engineering and Process Biotechnology

Enzyme activity was monitored over the last two stages of an enzyme extraction-separation process. 0.4 g protein, from Stage 5, converted 46 mmol substrate in 10 sec, and 0.02 g protein, from Stage 6, converted 49 mmol in 30 sec. Calculate the specific activities in units/g at each of the two steps 

TLS Online TPP Program

#Question id: 14364

#Section 5: Bioprocess Engineering and Process Biotechnology

Enzyme activity was monitored over the last two stages of an enzyme extraction-separation process. 0.4 g protein, from Stage 5, converted 46 mmol substrate in 10 sec, and 0.02 g protein, from Stage 6, converted 49 mmol in 30 sec. Calculate % increase in activity obtained over the two step  

TLS Online TPP Program

#Question id: 14365

#Section 5: Bioprocess Engineering and Process Biotechnology

0.1 mg of a quaternary structured enzyme (Mr 486 000) with four active sites converts 48 iimol substrate/10 sec. Calculate turnover number (min-1) 

TLS Online TPP Program

#Question id: 14366

#Section 5: Bioprocess Engineering and Process Biotechnology

0.1 mg of a quaternary structured enzyme (Mr 486 000) with four active sites converts 48 mirormol substrate/10 sec. Calculate molecular activity (min^-1), catalytic centre activity (min^-1). - 

TLS Online TPP Program

#Question id: 14367

#Section 5: Bioprocess Engineering and Process Biotechnology

During an enzyme purification, 0.23 g of protein was dissolved in 5 mL buffer. Suppose 0.5 mL of this solution converted 4.7 mmol of substrate in 30 sec. Calculate specific activity as units/mg protein - 

TLS Online TPP Program

#Question id: 14368

#Section 5: Bioprocess Engineering and Process Biotechnology

10 kg of a pure enzyme (Mr 30 000) catalyses the conversion of 1.5 g of a substrate (Mr 44) to products in 5 minutes. Calculate turnover number (sec^-1)  ....10^5