Kinetic study of a membrane enzyme reactor

✍ Scribed by H. Kitano; S. Yoshijima; S. Hotogi; N. Ise

• Publisher: John Wiley and Sons
• Year: 1980
• Tongue: English
• Weight: 395 KB
• Volume: 22
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/bit.260221211

✦ Synopsis

Abstract

A flat‐membrane dialyzer was used as enzyme reactor by introducing enzyme solution into one of the membrane‐separated chambers. The apparent Michaelis constant K~m~(app) of urease was always larger (ten times at [urease] = 1 mg/ml) than that of free enzyme because the permeation of substrate through the membrane was rate determining. K~m~(app) for urease decreased from 125 to 20m__M__ with increasing flow rate of the substrate solution because of the turbulent flow near the membrane. In the case of glucose oxidase or creatine kinase, the reaction rate was limited by the permeation of less permeable substrates such as oxygen or ATP. Therefore, K~m~(app) of more permeable substrates such as glucose or creatine became smaller than that of free enzyme. The reaction amount calculated from the permeation data agreed well with experimental results. By designing spacers for the reactor to give turbulence to the solution, the effectiveness of the reactor was improved fivefold.