Abstract
To evaluate the effectiveness of a ceramic monolith (mean pore diameter, 15 μm) as a support for the immobilized enzyme that catalyzes the hydrolysis of a high-molecular weight substrate, the hydrolysis of soluble starch (average molecular weight, 30 000) by use of glucoamylase from Rhizopus delemar was carried out at 50°C, pH 4.5. By observing the initial reaction rate in a batch reactor, wherein a fan-shaped piece of the immobilized enzyme monolith was fixed around a stirrer shaft, the pore diffusion resistance was found to be negligible when the concentration of starch exceeds 89 g/l. The simplified kinetic model, previously proposed, that assumed kinetic parameters as changing linearly with reduction of average molecular weight of substrate was also useful for simulating the immobilized enzyme system, regardless of batch or continuous mode, described in this paper.
| Original language | English |
|---|---|
| Pages (from-to) | 316-323 |
| Number of pages | 8 |
| Journal | kagaku kogaku ronbunshu |
| Volume | 9 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Jan 1 1983 |
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All Science Journal Classification (ASJC) codes
- Chemistry(all)
- Chemical Engineering(all)
Cite this
Hydrolysis of Soluble Starch by Glucoamylase Immobilized on Ceramic Monolith. / Shiraishi, Fumihide; Kawakami, Koei; Kato, Keiichi; Kusunoki, Koichiro.
In: kagaku kogaku ronbunshu, Vol. 9, No. 3, 01.01.1983, p. 316-323.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Hydrolysis of Soluble Starch by Glucoamylase Immobilized on Ceramic Monolith
AU - Shiraishi, Fumihide
AU - Kawakami, Koei
AU - Kato, Keiichi
AU - Kusunoki, Koichiro
PY - 1983/1/1
Y1 - 1983/1/1
N2 - To evaluate the effectiveness of a ceramic monolith (mean pore diameter, 15 μm) as a support for the immobilized enzyme that catalyzes the hydrolysis of a high-molecular weight substrate, the hydrolysis of soluble starch (average molecular weight, 30 000) by use of glucoamylase from Rhizopus delemar was carried out at 50°C, pH 4.5. By observing the initial reaction rate in a batch reactor, wherein a fan-shaped piece of the immobilized enzyme monolith was fixed around a stirrer shaft, the pore diffusion resistance was found to be negligible when the concentration of starch exceeds 89 g/l. The simplified kinetic model, previously proposed, that assumed kinetic parameters as changing linearly with reduction of average molecular weight of substrate was also useful for simulating the immobilized enzyme system, regardless of batch or continuous mode, described in this paper.
AB - To evaluate the effectiveness of a ceramic monolith (mean pore diameter, 15 μm) as a support for the immobilized enzyme that catalyzes the hydrolysis of a high-molecular weight substrate, the hydrolysis of soluble starch (average molecular weight, 30 000) by use of glucoamylase from Rhizopus delemar was carried out at 50°C, pH 4.5. By observing the initial reaction rate in a batch reactor, wherein a fan-shaped piece of the immobilized enzyme monolith was fixed around a stirrer shaft, the pore diffusion resistance was found to be negligible when the concentration of starch exceeds 89 g/l. The simplified kinetic model, previously proposed, that assumed kinetic parameters as changing linearly with reduction of average molecular weight of substrate was also useful for simulating the immobilized enzyme system, regardless of batch or continuous mode, described in this paper.
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UR - http://www.scopus.com/inward/citedby.url?scp=85004448454&partnerID=8YFLogxK
U2 - 10.1252/kakoronbunshu.9.316
DO - 10.1252/kakoronbunshu.9.316
M3 - Article
VL - 9
SP - 316
EP - 323
JO - Kagaku Kogaku Ronbunshu
JF - Kagaku Kogaku Ronbunshu
SN - 0386-216X
IS - 3
ER -