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Bioprocess Engineering 2nd Edition by Fikret Kargi,Michael Shuler
Edition 2ISBN: 9780130819086Bioprocess Engineering 2nd Edition by Fikret Kargi,Michael Shuler
Edition 2ISBN: 9780130819086 Exercise 4
a. H. H. Weetall and N. B. Havewala report the following data for the production of dex-
trose from corn starch using both soluble and immobilized (azo-glass beads) glucoamy-
lase in a fully agitated CSTR system.
1. Soluble data: T = 60∞C, [S0] = 168 mg starch/ml, [E0] = 11,600 units, volume = 1000 ml.
2. Immobilized data: T = 60∞C, [S0] = 336 mg starch/ml, [E0] = 46,400 units initially, im-
mobilized, volume = 1000 ml.
![a. H. H. Weetall and N. B. Havewala report the following data for the production of dex- trose from corn starch using both soluble and immobilized (azo-glass beads) glucoamy- lase in a fully agitated CSTR system. 1. Soluble data: T = 60∞C, [S0] = 168 mg starch/ml, [E0] = 11,600 units, volume = 1000 ml. 2. Immobilized data: T = 60∞C, [S0] = 336 mg starch/ml, [E0] = 46,400 units initially, im- mobilized, volume = 1000 ml. Determine the maximum reaction velocity, (mg/ml-min · unit of enzyme) and the satura- tion constant, (mg/ml). b. The same authors studied the effect of temperature on the maximum rate of the hydroly- sis of corn starch by glucoamylase. The results are tabulated next. Determine the activa- tion energy cal/g mole) for the soluble and immobilized enzyme reaction. c. Using these results, determine if immobilized enzyme is diffusion limited. [Courtesy of A. E. Humphrey from Collected Coursework Problems in Biochemical En- gineering compiled by H. W. Blanch for 1977 Am. Soc. Eng. Educ. Summer School.]](https://d2lvgg3v3hfg70.cloudfront.net/SM1185/11ec73a8_1d2b_9d10_b96d_4b6a164abefb_SM1185_00.jpg)
Determine the maximum reaction velocity,
![a. H. H. Weetall and N. B. Havewala report the following data for the production of dex- trose from corn starch using both soluble and immobilized (azo-glass beads) glucoamy- lase in a fully agitated CSTR system. 1. Soluble data: T = 60∞C, [S0] = 168 mg starch/ml, [E0] = 11,600 units, volume = 1000 ml. 2. Immobilized data: T = 60∞C, [S0] = 336 mg starch/ml, [E0] = 46,400 units initially, im- mobilized, volume = 1000 ml. Determine the maximum reaction velocity, (mg/ml-min · unit of enzyme) and the satura- tion constant, (mg/ml). b. The same authors studied the effect of temperature on the maximum rate of the hydroly- sis of corn starch by glucoamylase. The results are tabulated next. Determine the activa- tion energy cal/g mole) for the soluble and immobilized enzyme reaction. c. Using these results, determine if immobilized enzyme is diffusion limited. [Courtesy of A. E. Humphrey from Collected Coursework Problems in Biochemical En- gineering compiled by H. W. Blanch for 1977 Am. Soc. Eng. Educ. Summer School.]](https://d2lvgg3v3hfg70.cloudfront.net/SM1185/11ec73a8_1d2b_c421_b96d_9d151cfeb9fc_SM1185_00.jpg)
(mg/ml-min · unit of enzyme) and the satura-
tion constant,
![a. H. H. Weetall and N. B. Havewala report the following data for the production of dex- trose from corn starch using both soluble and immobilized (azo-glass beads) glucoamy- lase in a fully agitated CSTR system. 1. Soluble data: T = 60∞C, [S0] = 168 mg starch/ml, [E0] = 11,600 units, volume = 1000 ml. 2. Immobilized data: T = 60∞C, [S0] = 336 mg starch/ml, [E0] = 46,400 units initially, im- mobilized, volume = 1000 ml. Determine the maximum reaction velocity, (mg/ml-min · unit of enzyme) and the satura- tion constant, (mg/ml). b. The same authors studied the effect of temperature on the maximum rate of the hydroly- sis of corn starch by glucoamylase. The results are tabulated next. Determine the activa- tion energy cal/g mole) for the soluble and immobilized enzyme reaction. c. Using these results, determine if immobilized enzyme is diffusion limited. [Courtesy of A. E. Humphrey from Collected Coursework Problems in Biochemical En- gineering compiled by H. W. Blanch for 1977 Am. Soc. Eng. Educ. Summer School.]](https://d2lvgg3v3hfg70.cloudfront.net/SM1185/11ec73a8_1d2b_c422_b96d_8da924b17148_SM1185_00.jpg)
(mg/ml).
b. The same authors studied the effect of temperature on the maximum rate of the hydroly-
sis of corn starch by glucoamylase. The results are tabulated next. Determine the activa-
tion energy
![a. H. H. Weetall and N. B. Havewala report the following data for the production of dex- trose from corn starch using both soluble and immobilized (azo-glass beads) glucoamy- lase in a fully agitated CSTR system. 1. Soluble data: T = 60∞C, [S0] = 168 mg starch/ml, [E0] = 11,600 units, volume = 1000 ml. 2. Immobilized data: T = 60∞C, [S0] = 336 mg starch/ml, [E0] = 46,400 units initially, im- mobilized, volume = 1000 ml. Determine the maximum reaction velocity, (mg/ml-min · unit of enzyme) and the satura- tion constant, (mg/ml). b. The same authors studied the effect of temperature on the maximum rate of the hydroly- sis of corn starch by glucoamylase. The results are tabulated next. Determine the activa- tion energy cal/g mole) for the soluble and immobilized enzyme reaction. c. Using these results, determine if immobilized enzyme is diffusion limited. [Courtesy of A. E. Humphrey from Collected Coursework Problems in Biochemical En- gineering compiled by H. W. Blanch for 1977 Am. Soc. Eng. Educ. Summer School.]](https://d2lvgg3v3hfg70.cloudfront.net/SM1185/11ec73a8_1d2b_c423_b96d_b75cb9ff8a2b_SM1185_00.jpg)
cal/g mole) for the soluble and immobilized enzyme reaction.
![a. H. H. Weetall and N. B. Havewala report the following data for the production of dex- trose from corn starch using both soluble and immobilized (azo-glass beads) glucoamy- lase in a fully agitated CSTR system. 1. Soluble data: T = 60∞C, [S0] = 168 mg starch/ml, [E0] = 11,600 units, volume = 1000 ml. 2. Immobilized data: T = 60∞C, [S0] = 336 mg starch/ml, [E0] = 46,400 units initially, im- mobilized, volume = 1000 ml. Determine the maximum reaction velocity, (mg/ml-min · unit of enzyme) and the satura- tion constant, (mg/ml). b. The same authors studied the effect of temperature on the maximum rate of the hydroly- sis of corn starch by glucoamylase. The results are tabulated next. Determine the activa- tion energy cal/g mole) for the soluble and immobilized enzyme reaction. c. Using these results, determine if immobilized enzyme is diffusion limited. [Courtesy of A. E. Humphrey from Collected Coursework Problems in Biochemical En- gineering compiled by H. W. Blanch for 1977 Am. Soc. Eng. Educ. Summer School.]](https://d2lvgg3v3hfg70.cloudfront.net/SM1185/11ec73a8_1d2b_eb34_b96d_51c02d8b921a_SM1185_00.jpg)
c. Using these results, determine if immobilized enzyme is diffusion limited.
[Courtesy of A. E. Humphrey from "Collected Coursework Problems in Biochemical En-
gineering" compiled by H. W. Blanch for 1977 Am. Soc. Eng. Educ. Summer School.]
trose from corn starch using both soluble and immobilized (azo-glass beads) glucoamy-
lase in a fully agitated CSTR system.
1. Soluble data: T = 60∞C, [S0] = 168 mg starch/ml, [E0] = 11,600 units, volume = 1000 ml.
2. Immobilized data: T = 60∞C, [S0] = 336 mg starch/ml, [E0] = 46,400 units initially, im-
mobilized, volume = 1000 ml.
Determine the maximum reaction velocity,
(mg/ml-min · unit of enzyme) and the satura-tion constant,
(mg/ml).b. The same authors studied the effect of temperature on the maximum rate of the hydroly-
sis of corn starch by glucoamylase. The results are tabulated next. Determine the activa-
tion energy
cal/g mole) for the soluble and immobilized enzyme reaction. c. Using these results, determine if immobilized enzyme is diffusion limited.[Courtesy of A. E. Humphrey from "Collected Coursework Problems in Biochemical En-
gineering" compiled by H. W. Blanch for 1977 Am. Soc. Eng. Educ. Summer School.]
Explanation
Verified
Verified
a) Plotting 
versus data for both maxim...
Bioprocess Engineering 2nd Edition by Fikret Kargi,Michael Shuler
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