Study of an enzyme membrane reactor with immobilized fumarase for production of L-malic acid

Biotechnol Bioeng. 2001 Jan 5;72(1):77-84. doi: 10.1002/1097-0290(20010105)72:1<77::aid-bit11>3.0.co;2-l.

Abstract

The conversion of fumaric acid into L-malic acid by fumarase immobilized in a membrane reactor was analyzed experimentally. The enzyme was entrapped in asymmetric capillary membranes made of polysulfone. The performance of the reactor was evaluated in terms of conversion degree, reaction rate, and stability. The influence of operating conditions, such as amount of immobilized enzyme, substrate concentration, residence time, and axial flow rate, were investigated. The kinetic parameters K(m), V(max), and k(+2) were also measured. The stability of the immobilized enzyme was very good, showing no activity decay during more than 2 weeks of continuous operation.

MeSH terms

  • Animals
  • Bioreactors
  • Biotechnology / instrumentation
  • Biotechnology / methods
  • Capillary Action
  • Enzyme Stability
  • Enzymes, Immobilized / metabolism*
  • Equipment Design
  • Fumarate Hydratase / metabolism*
  • Kinetics
  • Malates / chemical synthesis*
  • Malates / metabolism
  • Myocardium / enzymology
  • Polymers
  • Sulfones
  • Swine

Substances

  • Enzymes, Immobilized
  • Malates
  • Polymers
  • Sulfones
  • polysulfone P 1700
  • malic acid
  • Fumarate Hydratase