Preparation and Properties of Gelatin-Immobilized β-Glucosidase from<i>Pyrococcus furiosus</i>

Nagatomo, Hidetaka; Matsushita, Yoh‐ichi; Sugamoto, Kazuhiro; Matsui, Takanao

doi:10.1271/bbb.69.128

Cited by 28 publications

(21 citation statements)

References 32 publications

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“…As the data from Nagamoto et al [15] indicates, thermostability of β-glucosidase immobilized on chitosan increases, and the enzyme works successfully at 70°C during 12 h. Such considerable increase of thermostability that we observed is due to the covalent binding of the enzyme and the carrier.…”

Section: Comparative Analysis Of Thermostability Of Native and Acetylsupporting

confidence: 70%

Immobilization of Fungal β-Glucosidase on Silica Gel and Kaolin Carriers

Karagulyan¹,

Gasparyan²,

Decker

2007

Appl Biochem Biotechnol

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Beta-glucosidase is a key enzyme in the hydrolysis of cellulose for producing feedstock glucose for various industrial processes. Reuse of enzyme through immobilization can significantly improve the economic characteristics of the process. Immobilization of the fungal beta-glucosidase by covalent binding and physical adsorption on silica gel and kaolin was conducted for consequent application of these procedures in large-scale industrial processes. Different immobilization parameters (incubation time, ionic strength, pH, enzyme/support ratio, glutaric aldehyde concentration, etc.) were evaluated for their effect on the thermal stability of the immobilized enzyme. It was shown that the immobilized enzyme activity is stable at 50 degrees C over 8 days. It has also been shown that in the case of immobilization on kaolin, approximately 95% of the initial enzyme was immobilized onto support, and loss of activity was not observed. However, covalent binding of the enzyme to silica gel brings significant loss of enzyme activity, and only 35% of activity was preserved. In the case of physical adsorption on kaolin, gradual desorption of enzyme takes place. To prevent this process, we have carried out chemical modification of the protein. As a result, after repeated washings, enzyme desorption from kaolin has been reduced from 75 to 20-25% loss.

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Section: Comparative Analysis Of Thermostability Of Native and Acetylsupporting

confidence: 70%

Immobilization of Fungal β-Glucosidase on Silica Gel and Kaolin Carriers

Karagulyan¹,

Gasparyan²,

Decker

2007

Appl Biochem Biotechnol

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“…-glucosidase activity was determined using -nitrophenyl -D-glucopyranoside ( NPG), 20,21) 4-hydroxyphenyl -D-glucopyranoside (arbutin), 2-(hydroxymethyl) phenyl -D-glucopyranoside (salicin), and 4-methylumbelliferyl -D-glucoside (MUG) 22) as substrates. The standard assay consisted of incubating enzyme with 5 mM NPG in 50 mM sodium phosphate buffer (pH 7.0) for 10 min in a total volume of 0.5 ml.…”

Section: Methodsmentioning

confidence: 99%

Cloning and Comparison of Third β-Glucoside Utilization (bglEFIA) Operon with Two Operons ofPectobacterium carotovorumsubsp.carotovorumLY34

Hong¹,

An²,

Cho³

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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“…The classic analytical method reported for the measurement of ␤-glucosidase activity was spectrophotometry, and p-nitrophenol was monitored at 403 nm [10][11][12], where pnitrophenyl ␤-d-glucopyranoside had no absorption. In the present study, considering the sample volume required for spectrophotometry, there was not enough homogenate for some rat tissues, such as bladder, thymus, esophagus, etc.…”

Section: Methodsmentioning

confidence: 99%