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Glucoamylase immobilized on acid‐hydrolyzed starch graft polyacrylonitrile
Author(s) -
Slininger P. J.,
Fanta G. F.,
Abbott T. P.
Publication year - 1988
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.260310802
Subject(s) - maltose , hydrolysis , polyacrylonitrile , starch , chemistry , substrate (aquarium) , immobilized enzyme , enzyme , polysaccharide , chromatography , product inhibition , biochemistry , organic chemistry , non competitive inhibition , polymer , biology , ecology
Abstract A continuous stirred reactor fed maltose as substrate was used to show that acid hydrolyzed starch‐g‐polyacry‐lonitrile and other polysaccharide graft copolymers can bind and retain significant quantities of active glucoamy‐lase. Glucose productivities up to 2.7 g/g carrier/h were observed with the immobilized glucoamylase, and half‐lives up to 1800 h were indicative of activity longevity. Factors influencing the immobilized enzyme activity and first‐order decay rate included temperature, p H , and carrier composition. In all cases, maltose was converted quantitatively to glucose with no evidence of reversion product formation.