Repeated hydrolysis of raw starch using amylase immobilized on a reversibly soluble-insoluble carrier.

Hoshino, Kazuhiro; Taniguchi, Masayuki; Netsu, Yoshiaki; Fujii, Michihiro

doi:10.1252/jcej.22.54

Cited by 34 publications

(14 citation statements)

References 13 publications

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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%

A Fractal-Like Kinetic Equation to Investigate Temperature Effect on Cellulose Hydrolysis by Free and Immobilized Cellulase

Zhang

et al. 2011

Appl Biochem Biotechnol

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According to fractal-like theory in the heterogeneous system, a cellulase-catalyzed kinetic equation that contained two parameters (rate constant k and fractal dimension h) was deduced. The equation described directly the mathematical relationship between reducing sugar concentration and hydrolytic time, and accurately fitted the experimental data of free/immobilized cellulase at 37, 40, 44, 47, and 50 °C (R(2)>0.99). The fitted h value is estimated as a constant (0.6148) in these tested temperatures. The fitted k value increased with temperature increase, and the relationship agreed with Arrhenius equation (R(2)>0.98). The fractal-like equation could predict accurately the experimental data at low temperature 34 °C for free/immobilized cellulase and high temperature 53 °C for immobilized cellulase, but the prediction at 53 °C for free cellulase was not accurate enough due to its lower stability than immobilized cellulase. The application of fractal-like theory in cellulase kinetics is successful.

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Section: Arrhenius Equation Based Fitmentioning

confidence: 99%

A Fractal-Like Kinetic Equation to Investigate Temperature Effect on Cellulose Hydrolysis by Free and Immobilized Cellulase

Zhang

et al. 2011

Appl Biochem Biotechnol

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“…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%

Repeated Batch Conversion of Raw Starch to Ethanol Using Amylase Immobilized on a Reversible Soluble-autoprecipitating Carrier and Flocculating Yeast Cells

Hoshino¹,

Taniguchi²,

Marumoto³

et al. 1989

Agricultural and Biological Chemistry

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“…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%

An update on smart biocatalysts for industrial and biomedical applications

Shakya

Nandakumar

2018

J. R. Soc. Interface.

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Recently, smart biocatalysts, where enzymes are conjugated to stimuli-responsive (smart) polymers, have gained significant attention. Based on the presence or absence of external stimuli, the polymer attached to the enzyme changes its conformation to protect the enzyme from the external environment and regulate the enzyme activity, thus acting as a molecular switch. Owing to this behaviour, smart biocatalysts can be separated easily from a reaction mixture and re-used several times. Several such smart polymer-based biocatalysts have been developed for industrial and biomedical applications. In addition, they have been used in biosensors, biometrics and nano-electronic devices. This review article covers recent advances in developing different kinds of stimuli-responsive enzyme bioconjugates, including conjugation strategies, and their applications.

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Repeated hydrolysis of raw starch using amylase immobilized on a reversibly soluble-insoluble carrier.

Cited by 34 publications

References 13 publications

A Fractal-Like Kinetic Equation to Investigate Temperature Effect on Cellulose Hydrolysis by Free and Immobilized Cellulase

A Fractal-Like Kinetic Equation to Investigate Temperature Effect on Cellulose Hydrolysis by Free and Immobilized Cellulase

Repeated Batch Conversion of Raw Starch to Ethanol Using Amylase Immobilized on a Reversible Soluble-autoprecipitating Carrier and Flocculating Yeast Cells

An update on smart biocatalysts for industrial and biomedical applications

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