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book Bioprocess Engineering 2nd Edition by Fikret Kargi,Michael Shuler cover

Bioprocess Engineering 2nd Edition by Fikret Kargi,Michael Shuler

Edition 2ISBN: 9780130819086
book Bioprocess Engineering 2nd Edition by Fikret Kargi,Michael Shuler cover

Bioprocess 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.]
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.] (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.] (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.] 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.] 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
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Bioprocess Engineering 2nd Edition by Fikret Kargi,Michael Shuler
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