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Immobilization of enzymes based on hydrophobic interaction. III. Adsorbent substituent density and its impact on the immobilization of β‐amylase
Author(s) -
Caldwell Karin Dahlgren,
Axén Rolf,
Bergwall Margareta,
Olsson Ingmar,
Porath Jerker
Publication year - 1976
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260181109
Subject(s) - chemistry , maltose , adsorption , galactose , substituent , starch , amylase , substrate (aquarium) , chromatography , immobilized enzyme , sepharose , enzyme , organic chemistry , polymer chemistry , oceanography , geology
Hexyl‐groups have been introduced into crosslinked Sepharose 6B, yielding gels with degrees of substitution which range from 0.02 to 0.70 mol hexyl‐side chain per mole galactose residue. The gels were exposed to β‐amylase in solution, and the resulting adsorbates indicated a monotonic increase in adsorption capacity with an increasing hexyl‐content. Adsorbate activity, by contrast, displayed a maximum for a carrier gel with a hexyl–galactose ratio of 0.51. Adsorbates based on gels with different hexyl‐content were used in column reactors for continuous maltose production from a soluble starch substrate.