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Production and Properties of an Immobilized Glucose Isomerase
Author(s) -
Hupkes J. V.,
van Tilburg R.
Publication year - 1976
Publication title -
starch ‐ stärke
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.62
H-Index - 82
eISSN - 1521-379X
pISSN - 0038-9056
DOI - 10.1002/star.19760281008
Subject(s) - glutaraldehyde , glucose 6 phosphate isomerase , immobilized enzyme , substrate (aquarium) , chromatography , chemistry , enzyme , solvent , flux (metallurgy) , chemical engineering , organic chemistry , oceanography , engineering , geology
The enzyme glucose isomerase used by Gist‐Brocades for the process of immobilization is derived from a strain of Actinoplanes missouriensis . The intracellular enzyme is fixed to the mycelium and as such immobilized. In the immobilization procedure an enzyme gelatine mixture is sprayed into a cold water‐immiscible organic solvent and the particles so formed are separated and thoroughly washed. Subsequently the so occlused enzyme particles are cross‐linked in a solution of glutaraldehyde. The particles are washed again and finally stored in solution or dried. The immobilized glucose isomerase — MAXAZYME® GI‐IMMOB — consists of spherical brown‐coloured particles. The diameter of the particles is about 1 mm. The enzyme particles can be used in column, batch, continuous feed and stirred tank and fluid bed reactors. The optimal performance conditions e. g. temperature, pH, substrate flux, half, life value and hold up time are described.