Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supports
| ISSN: |
0006-3592
|
|---|---|
| Keywords: |
Chemistry ; Biochemistry and Biotechnology
|
| Source: |
Wiley InterScience Backfile Collection 1832-2000
|
| Topics: |
Biology
Process Engineering, Biotechnology, Nutrition Technology
|
| Notes: |
Glucoamylase from four different companies was studied: three had similar stability (half-life at 50°C about 140 hr); the fourth was less stable (half-life at 50°C about 20 hr). The immobilized enzymes were all less stable than their soluble counterparts: immobilized enzyme stability depended on the soluble enzyme used, the support, and method of immobilization. Thus enzyme bound to Enzacryl-TIO was less stable than enzyme bound to hornblende (metal-link method); this, in turn, was less stable than enzyme bound to hornblende by a silane-glutaraldehyde process. Bound enzyme stability was also improved by the presence of substrate or product (starch maltose or glucose). After 110 hr at 50°C in the presence of maltose (10% (w/v)) one preparation (a more stable soluble enzyme boul1d to hornblende by a silane-glutaraldehyde process) retained over 95% of its activity: activity loss was too low to permit the estimation of a half-life.
|
| Additional Material: |
4 Ill.
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798297794498265092 |
|---|---|
| addmaterial | 4 Ill. |
| autor | Flynn, A. Johnson, D. B. |
| autorsonst | Flynn, A. Johnson, D. B. |
| book_url | http://dx.doi.org/10.1002/bit.260200909 |
| datenlieferant | nat_lic_papers |
| hauptsatz | hsatz_simple |
| identnr | NLM159614643 |
| issn | 0006-3592 |
| journal_name | Biotechnology and Bioengineering |
| materialart | 1 |
| notes | Glucoamylase from four different companies was studied: three had similar stability (half-life at 50°C about 140 hr); the fourth was less stable (half-life at 50°C about 20 hr). The immobilized enzymes were all less stable than their soluble counterparts: immobilized enzyme stability depended on the soluble enzyme used, the support, and method of immobilization. Thus enzyme bound to Enzacryl-TIO was less stable than enzyme bound to hornblende (metal-link method); this, in turn, was less stable than enzyme bound to hornblende by a silane-glutaraldehyde process. Bound enzyme stability was also improved by the presence of substrate or product (starch maltose or glucose). After 110 hr at 50°C in the presence of maltose (10% (w/v)) one preparation (a more stable soluble enzyme boul1d to hornblende by a silane-glutaraldehyde process) retained over 95% of its activity: activity loss was too low to permit the estimation of a half-life. |
| package_name | Wiley-Blackwell |
| publikationsjahr_anzeige | 1978 |
| publikationsjahr_facette | 1978 |
| publikationsjahr_intervall | 8024:1975-1979 |
| publikationsjahr_sort | 1978 |
| publikationsort | New York, NY [u.a.] |
| publisher | Wiley-Blackwell |
| reference | 20 (1978), S. 1445-1454 |
| schlagwort | Chemistry Biochemistry and Biotechnology |
| search_space | articles |
| shingle_author_1 | Flynn, A. Johnson, D. B. |
| shingle_author_2 | Flynn, A. Johnson, D. B. |
| shingle_author_3 | Flynn, A. Johnson, D. B. |
| shingle_author_4 | Flynn, A. Johnson, D. B. |
| shingle_catch_all_1 | Flynn, A. Johnson, D. B. Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supports Chemistry Biochemistry and Biotechnology Chemistry Biochemistry and Biotechnology Glucoamylase from four different companies was studied: three had similar stability (half-life at 50°C about 140 hr); the fourth was less stable (half-life at 50°C about 20 hr). The immobilized enzymes were all less stable than their soluble counterparts: immobilized enzyme stability depended on the soluble enzyme used, the support, and method of immobilization. Thus enzyme bound to Enzacryl-TIO was less stable than enzyme bound to hornblende (metal-link method); this, in turn, was less stable than enzyme bound to hornblende by a silane-glutaraldehyde process. Bound enzyme stability was also improved by the presence of substrate or product (starch maltose or glucose). After 110 hr at 50°C in the presence of maltose (10% (w/v)) one preparation (a more stable soluble enzyme boul1d to hornblende by a silane-glutaraldehyde process) retained over 95% of its activity: activity loss was too low to permit the estimation of a half-life. 0006-3592 00063592 Wiley-Blackwell |
| shingle_catch_all_2 | Flynn, A. Johnson, D. B. Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supports Chemistry Biochemistry and Biotechnology Chemistry Biochemistry and Biotechnology Glucoamylase from four different companies was studied: three had similar stability (half-life at 50°C about 140 hr); the fourth was less stable (half-life at 50°C about 20 hr). The immobilized enzymes were all less stable than their soluble counterparts: immobilized enzyme stability depended on the soluble enzyme used, the support, and method of immobilization. Thus enzyme bound to Enzacryl-TIO was less stable than enzyme bound to hornblende (metal-link method); this, in turn, was less stable than enzyme bound to hornblende by a silane-glutaraldehyde process. Bound enzyme stability was also improved by the presence of substrate or product (starch maltose or glucose). After 110 hr at 50°C in the presence of maltose (10% (w/v)) one preparation (a more stable soluble enzyme boul1d to hornblende by a silane-glutaraldehyde process) retained over 95% of its activity: activity loss was too low to permit the estimation of a half-life. 0006-3592 00063592 Wiley-Blackwell |
| shingle_catch_all_3 | Flynn, A. Johnson, D. B. Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supports Chemistry Biochemistry and Biotechnology Chemistry Biochemistry and Biotechnology Glucoamylase from four different companies was studied: three had similar stability (half-life at 50°C about 140 hr); the fourth was less stable (half-life at 50°C about 20 hr). The immobilized enzymes were all less stable than their soluble counterparts: immobilized enzyme stability depended on the soluble enzyme used, the support, and method of immobilization. Thus enzyme bound to Enzacryl-TIO was less stable than enzyme bound to hornblende (metal-link method); this, in turn, was less stable than enzyme bound to hornblende by a silane-glutaraldehyde process. Bound enzyme stability was also improved by the presence of substrate or product (starch maltose or glucose). After 110 hr at 50°C in the presence of maltose (10% (w/v)) one preparation (a more stable soluble enzyme boul1d to hornblende by a silane-glutaraldehyde process) retained over 95% of its activity: activity loss was too low to permit the estimation of a half-life. 0006-3592 00063592 Wiley-Blackwell |
| shingle_catch_all_4 | Flynn, A. Johnson, D. B. Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supports Chemistry Biochemistry and Biotechnology Chemistry Biochemistry and Biotechnology Glucoamylase from four different companies was studied: three had similar stability (half-life at 50°C about 140 hr); the fourth was less stable (half-life at 50°C about 20 hr). The immobilized enzymes were all less stable than their soluble counterparts: immobilized enzyme stability depended on the soluble enzyme used, the support, and method of immobilization. Thus enzyme bound to Enzacryl-TIO was less stable than enzyme bound to hornblende (metal-link method); this, in turn, was less stable than enzyme bound to hornblende by a silane-glutaraldehyde process. Bound enzyme stability was also improved by the presence of substrate or product (starch maltose or glucose). After 110 hr at 50°C in the presence of maltose (10% (w/v)) one preparation (a more stable soluble enzyme boul1d to hornblende by a silane-glutaraldehyde process) retained over 95% of its activity: activity loss was too low to permit the estimation of a half-life. 0006-3592 00063592 Wiley-Blackwell |
| shingle_title_1 | Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supports |
| shingle_title_2 | Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supports |
| shingle_title_3 | Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supports |
| shingle_title_4 | Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supports |
| sigel_instance_filter | dkfz geomar wilbert ipn albert |
| source_archive | Wiley InterScience Backfile Collection 1832-2000 |
| timestamp | 2024-05-06T10:13:39.761Z |
| titel | Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supports |
| titel_suche | Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supports |
| topic | W ZM |
| uid | nat_lic_papers_NLM159614643 |