Effects of mass-transfer resistance on apparent stability and performance of fixed-bed immobilized enzyme reactors: theory and experiments with immobilized invertase

Journal Article · Sat Jan 01 00:00:00 EST 1983 · Biotechnol. Bioeng.; (United States)

DOI:https://doi.org/10.1002/bit.260250112· OSTI ID:5423619

Ooshima, H; Harano, Y

Taking the hydrolysis of sucrose by invertase immobilized on anion-exchange resin as an example, the effects of mass-transfer resistance on the apparent stability of immobilized enzyme (IME) and the optimal policy for an IME reaction in a fixed-bed reactor have been studied theoretically and experimentally. The following results were obtained: 1) The effect of mass-transfer resistance on the effective deactivation rate of IME is summarized in two parameters concerning the intraparticle diffusion alphap and the interparticle alphaf. 2) At a constant processed amount of raw materials, there exists an optimal flow rate of reaction fluid to enhance the reactor performance while the mass-transfer resistance shifts the optimal point. 3) The intrinsic deactivation rate of IME has been estimated from the relationship between the fractional conversion at the reactor outlet and the operation time. (Refs. 12).

• Research Organization: Dept. of Applied Chemistry, Faculty of Engineering, Osaka City Univ., Osaka 558, Japan
• OSTI ID: 5423619
• Journal Information: Biotechnol. Bioeng.; (United States), Vol. 25:1
• Country of Publication: United States
• Language: English

Related Subjects

09 BIOMASS FUELS
SACCHAROSE
ENZYMATIC HYDROLYSIS
BIOCHEMICAL REACTION KINETICS
BIOREACTORS
CHEMICAL REACTORS
IMMOBILIZED ENZYMES
MASS TRANSFER
PACKED BED
CARBOHYDRATES
CHEMICAL REACTIONS
DECOMPOSITION
DISACCHARIDES
HYDROLYSIS
KINETICS
LYSIS
OLIGOSACCHARIDES
ORGANIC COMPOUNDS
REACTION KINETICS
SACCHARIDES
SOLVOLYSIS
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