Glucose oxidase immobilized on eupergit C and CPG-10 a comparison

Wehnert, G.; Sauerbrei, A.; Schügerl, K.

doi:10.1007/bf01025564

Cited by 13 publications

(3 citation statements)

References 2 publications

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“…The actual bonding of the enzyme to the film could at worst cause it to lose 2 0 4 0 % of its activity, so the amount would have to be further increased, perhaps offsetting the lower temperature diffusion advantage. Once the enzyme is bound it should have fairly good stability over the 30-60 days needed when it is activated in the presence of water (Wehnert et al 1985).…”

Section: Glucose Oxidase Enzyme Oxygen Scavenger Systemmentioning

confidence: 99%

“…A major unknown factor is how stable the enzyme will be on the film over time. Wehnert et al (1985) showed that glucose oxidase bound to a plastic surface (Eupergit C) underwent a 50% drop in activity in 2-3 weeks followed by little loss over the next 4 weeks. Hartmeier (1979) and Hartmeier and Tegge (1979) reported on a fairly stable preparation in a gelatin gel matrix hardened with glutaraldehyde and formaldehyde.…”

Section: Glucose Oxidase Enzyme Oxygen Scavenger Systemmentioning

confidence: 99%

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Applications of "Active Packaging" for Improvement of Shelf-Life and Nutritional Quality of Fresh and Extended Shelf-Life Foods

Labuza

Breene

1989

J Food Processing Preservation

366

128

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Section: Glucose Oxidase Enzyme Oxygen Scavenger Systemmentioning

confidence: 99%

Section: Glucose Oxidase Enzyme Oxygen Scavenger Systemmentioning

confidence: 99%

Applications of "Active Packaging" for Improvement of Shelf-Life and Nutritional Quality of Fresh and Extended Shelf-Life Foods

Labuza

Breene

1989

J Food Processing Preservation

366

128

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“…Xylose and XOS (X2, X3, X4 and X5) were used as standards. Since the retention time of X2 and hexose was the same by the HPLC, the amount of X2 was determined by removing the amount of hexose (glucose and galactose) by colorimetric analysis of GOD-POD (detection limit: 0.05 mg/ml) [31] and galactose detection kit (detection limit: 0.04 mg/ml) (Arbor Assays, Ann Arbor, MI, USA). The amounts of unknown components (U1, U2 and U3) were determined by xylose as standard.…”

Section: Enzymatic Production and Evaluation Of Xosmentioning

confidence: 99%

Enzymatic production of xylooligosaccharides from red alga dulse (Palmaria sp.) wasted in Japan

Yamamoto

Kishimura

Kinoshita³

et al. 2019

Process Biochemistry

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Red alga dulse (Palmaria sp.) has xylan with a small amount of cellulose and less lignin, hence these characteristics may provide some advantages in the enzymatic production of xylooligosaccharides (XOS). To evaluate dulse xylan as XOS source, we prepared xylan rich fraction (DXRF) and attempted XOS production using commercial enzymes. 13.8% of xylan rich fraction (DXRF: containing 52.2% of xylan) was obtained from dried dulse powder. We then evaluated the hydrolysis products of two commercial enzymes, revealing that hydrolysate of Hemicellulase amano 90 contained less xylose. The effective XOS production by the enzyme was evaluated in terms of enzyme dose, DXRF concentration and reaction period, showing that 66.6% of XOS was obtained from DXRF with the hydrolysis rate of 82% under the following condition: 54 U Hemicellulase amano 90, 10 mg/ml DXRF, pH 4.5, 50 o C for 24 h. These results indicated that red algae xylan is suitable for XOS source.

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Continuous‐flow bioluminescent dtermination of ATP in platelets using firefly luciferase immobilized on epoxy methacrylate

Carrea

Bovara

Girotti

et al. 1989

J. Biolumin. Chemilumin.

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Firefly luciferase was immobilized on epoxy methacrylate beads and used for a continuous-flow assay of ATP extracted from platelets. The immobilized luciferase had a half-life of 3 days at 25 degrees C; there was a 25% recovery of luciferase activity upon immobilization, and ca 50 reactors were made from 1 mg of commercial enzyme. The sensitivity of the assay was 0.3 pmol of ATP, and the response was linear between 1 and 500 pmol of ATP. The ATP content of platelets obtained with the present method correlated well with those obtained using soluble luciferase.

show abstract

Glucose oxidase immobilized on eupergit C and CPG-10 a comparison

Cited by 13 publications

References 2 publications

Applications of "Active Packaging" for Improvement of Shelf-Life and Nutritional Quality of Fresh and Extended Shelf-Life Foods

Applications of "Active Packaging" for Improvement of Shelf-Life and Nutritional Quality of Fresh and Extended Shelf-Life Foods

Enzymatic production of xylooligosaccharides from red alga dulse (Palmaria sp.) wasted in Japan

Continuous‐flow bioluminescent dtermination of ATP in platelets using firefly luciferase immobilized on epoxy methacrylate

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