The immobilisation of invertase on Hornblende and on Enzacryl TIO: Optimisation and stability studies

Albert  Flynn; D. B. Johnson

doi:10.1016/0020-711X(77)90155-0

The immobilisation of invertase on Hornblende and on Enzacryl TIO: Optimisation and stability studies

Albert Flynn
, D. B. Johnson

School of Food and Nutritional Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

1. Invertase immobilized on hornblende was more active, and more stable at 45°C, than that on Enzacryl-TIO.

2. Highest activities were obtained with a crude particulate enzyme preparation, rather than with purified preparations.

3. At 60°C hornblende-bound enzyme had comparable stability to that of soluble enzyme, but the presence of substrate increased the stability of the bound enzyme.

4. Enzacryl-TIO-invertase had greater physical stability than hornblende-invertase.

Original language	English (Ireland)
Pages (from-to)	243-247
Journal	International Journal of Biochemistry
Volume	8
Issue number	3
DOIs	https://doi.org/10.1016/0020-711X(77)90155-0
Publication status	Published - 1977

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title = "The immobilisation of invertase on Hornblende and on Enzacryl TIO: Optimisation and stability studies",

abstract = "1. Invertase immobilized on hornblende was more active, and more stable at 45°C, than that on Enzacryl-TIO. 2. Highest activities were obtained with a crude particulate enzyme preparation, rather than with purified preparations. 3. At 60°C hornblende-bound enzyme had comparable stability to that of soluble enzyme, but the presence of substrate increased the stability of the bound enzyme. 4. Enzacryl-TIO-invertase had greater physical stability than hornblende-invertase.",

author = "Albert Flynn and Johnson, \{D. B.\}",

year = "1977",

doi = "10.1016/0020-711X(77)90155-0",

language = "English (Ireland)",

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pages = "243--247",

journal = "International Journal of Biochemistry",

issn = "0020-711X",

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T1 - The immobilisation of invertase on Hornblende and on Enzacryl TIO

T2 - Optimisation and stability studies

AU - Flynn, Albert

AU - Johnson, D. B.

PY - 1977

Y1 - 1977

N2 - 1. Invertase immobilized on hornblende was more active, and more stable at 45°C, than that on Enzacryl-TIO. 2. Highest activities were obtained with a crude particulate enzyme preparation, rather than with purified preparations. 3. At 60°C hornblende-bound enzyme had comparable stability to that of soluble enzyme, but the presence of substrate increased the stability of the bound enzyme. 4. Enzacryl-TIO-invertase had greater physical stability than hornblende-invertase.

AB - 1. Invertase immobilized on hornblende was more active, and more stable at 45°C, than that on Enzacryl-TIO. 2. Highest activities were obtained with a crude particulate enzyme preparation, rather than with purified preparations. 3. At 60°C hornblende-bound enzyme had comparable stability to that of soluble enzyme, but the presence of substrate increased the stability of the bound enzyme. 4. Enzacryl-TIO-invertase had greater physical stability than hornblende-invertase.

U2 - 10.1016/0020-711X(77)90155-0

DO - 10.1016/0020-711X(77)90155-0

M3 - Article

SN - 0020-711X

VL - 8

SP - 243

EP - 247

JO - International Journal of Biochemistry

JF - International Journal of Biochemistry

IS - 3

ER -

The immobilisation of invertase on Hornblende and on Enzacryl TIO: Optimisation and stability studies

Abstract

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