1989
DOI: 10.1252/jcej.22.54
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Repeated hydrolysis of raw starch using amylase immobilized on a reversibly soluble-insoluble carrier.

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Cited by 34 publications
(14 citation statements)
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“…Via the immobilization, the affinity of enzyme to substrate could be improved as others demonstrated [36,37]. It also has been reported that coupling enzyme to other smart polymers could improve the affinity [38][39][40][41][42][43]. E a is the minimum required potential energy for conversion of the reactants to the activated complex.…”
Section: Arrhenius Equation Based Fitmentioning
confidence: 99%
“…Via the immobilization, the affinity of enzyme to substrate could be improved as others demonstrated [36,37]. It also has been reported that coupling enzyme to other smart polymers could improve the affinity [38][39][40][41][42][43]. E a is the minimum required potential energy for conversion of the reactants to the activated complex.…”
Section: Arrhenius Equation Based Fitmentioning
confidence: 99%
“…To clarify the effectiveness of the use of D-AS in a soluble state, the specific activities per amount of enzyme protein for raw starch and three kinds of soluble substrates were compared with our previous results 8 ) on the native Table I, there was little significant difference in the specific activity for maltose between ND and two types of the immobilized Dabiase. The apparent activities of D-AS for not only dextrin and soluble starch but also raw starch were more than 70% those of ND.…”
Section: Substrate Specificitymentioning
confidence: 98%
“…This transition occurs due to changes in electrostatic interactions along the polymer backbone. These changes cause the ionization and deionization of functional moieties of the polymer [1,2] [49]. Later, the same group synthesized another reversible pH-sensitive hydroxypropyl methylcellulose acetate succinate polymer-based amylase conjugate with entrapped Lactobacillus bacteria for continuous catalysis of starch for lactic acid production.…”
Section: Industrial Biocatalystsmentioning
confidence: 99%
“…Among several polymers, Eduragit L-100 was most stable and it was soluble above pH 5.0 while precipitating at pH 3.5. The specific activity of the Eudragit-based bioconjugate was approximately 85% of the free enzyme activity [49]. Later, the same group synthesized another reversible pH-sensitive hydroxypropyl methylcellulose acetate succinate polymer-based amylase conjugate with entrapped Lactobacillus bacteria for continuous catalysis of starch for lactic acid production.…”
Section: Industrial Biocatalystsmentioning
confidence: 99%