Immobilized glucoamylase: Studies on Hornblende and Enzacryl TIO

Albert  Flynn; D. B. Johnson

doi:10.1016/0020-711X(77)90111-2

Immobilized glucoamylase: Studies on Hornblende and Enzacryl TIO

Albert Flynn
, D. B. Johnson

School of Food and Nutritional Sciences

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

Abstract

1. Partially purified glucoamylase was immobilized on hornblende particles with a 4-fold increase in activity over previous such preparations.

2. Enzacryl-T10-bound enzyme was more active than hornblende-bound enzyme, while the latter had the greater stability at 50°C.

3. The thermal stability of either preparation was less than that of the soluble enzyme.

Original language	English (Ireland)
Pages (from-to)	501-503
Journal	International Journal of Biochemistry
Volume	8
Issue number	7
DOIs	https://doi.org/10.1016/0020-711X(77)90111-2
Publication status	Published - 1977

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@article{4103b27c660841df947b929897eaac0a,

title = "Immobilized glucoamylase: Studies on Hornblende and Enzacryl TIO",

abstract = "1. Partially purified glucoamylase was immobilized on hornblende particles with a 4-fold increase in activity over previous such preparations. 2. Enzacryl-T10-bound enzyme was more active than hornblende-bound enzyme, while the latter had the greater stability at 50°C. 3. The thermal stability of either preparation was less than that of the soluble enzyme.",

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

year = "1977",

doi = "10.1016/0020-711X(77)90111-2",

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AU - Flynn, Albert

AU - Johnson, D. B.

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N2 - 1. Partially purified glucoamylase was immobilized on hornblende particles with a 4-fold increase in activity over previous such preparations. 2. Enzacryl-T10-bound enzyme was more active than hornblende-bound enzyme, while the latter had the greater stability at 50°C. 3. The thermal stability of either preparation was less than that of the soluble enzyme.

AB - 1. Partially purified glucoamylase was immobilized on hornblende particles with a 4-fold increase in activity over previous such preparations. 2. Enzacryl-T10-bound enzyme was more active than hornblende-bound enzyme, while the latter had the greater stability at 50°C. 3. The thermal stability of either preparation was less than that of the soluble enzyme.

U2 - 10.1016/0020-711X(77)90111-2

DO - 10.1016/0020-711X(77)90111-2

M3 - Article

SN - 0020-711X

VL - 8

SP - 501

EP - 503

JO - International Journal of Biochemistry

JF - International Journal of Biochemistry

IS - 7

ER -

Immobilized glucoamylase: Studies on Hornblende and Enzacryl TIO

Abstract

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