Isolation of β-Xylanase from whole broth of Bacillus amyloliquefaciens by adsorption on a matrix in fluidized bed with low degree of expansion
Abstract β-1,4-Xylanase, produced extracellularly by Bacillus amyloliquefaciens MIR 32, was isolated directly from the culture broth by adsorption on a cation exchanger, Amberlite IRC-50, in fluidized bed with a low degree of expansion. The enzyme was eluted from the adsorbent by increase in pH, wit...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Breccia, Javier D. [verfasserIn] |
|---|
| Format: |
Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1999 |
|---|
| Anmerkung: |
© Kluwer Academic Publishers 1999 |
|---|
| Übergeordnetes Werk: |
Enthalten in: Bioseparation - Kluwer Academic Publishers, 1990, 8(1999), 6 vom: Nov., Seite 273-280 |
|---|---|
| Übergeordnetes Werk: |
volume:8 ; year:1999 ; number:6 ; month:11 ; pages:273-280 |
| Links: |
|---|
| DOI / URN: |
10.1023/A:1008174513826 |
|---|
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OLC205051218X |
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| 520 | |a Abstract β-1,4-Xylanase, produced extracellularly by Bacillus amyloliquefaciens MIR 32, was isolated directly from the culture broth by adsorption on a cation exchanger, Amberlite IRC-50, in fluidized bed with a low degree of expansion. The enzyme was eluted from the adsorbent by increase in pH, with a recovery of 82.3% and purification of 5.3 fold. About 99.99% of the colony forming units, 82% of the contaminating neutral protease activity, and 100% of the reducing sugars present in the crude feedstock were removed at the end of the purification cycle. | ||
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10.1023/A:1008174513826 doi (DE-627)OLC205051218X (DE-He213)A:1008174513826-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn Breccia, Javier D. verfasserin aut Isolation of β-Xylanase from whole broth of Bacillus amyloliquefaciens by adsorption on a matrix in fluidized bed with low degree of expansion 1999 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Kluwer Academic Publishers 1999 Abstract β-1,4-Xylanase, produced extracellularly by Bacillus amyloliquefaciens MIR 32, was isolated directly from the culture broth by adsorption on a cation exchanger, Amberlite IRC-50, in fluidized bed with a low degree of expansion. The enzyme was eluted from the adsorbent by increase in pH, with a recovery of 82.3% and purification of 5.3 fold. About 99.99% of the colony forming units, 82% of the contaminating neutral protease activity, and 100% of the reducing sugars present in the crude feedstock were removed at the end of the purification cycle. Hatti-Kaul, Rajni aut Castro, Guillermo R. aut Siñeriz, Faustino aut Enthalten in Bioseparation Kluwer Academic Publishers, 1990 8(1999), 6 vom: Nov., Seite 273-280 (DE-627)130868930 (DE-600)1033272-8 (DE-576)063974134 0923-179X nnns volume:8 year:1999 number:6 month:11 pages:273-280 https://doi.org/10.1023/A:1008174513826 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_65 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_4012 AR 8 1999 6 11 273-280 |
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10.1023/A:1008174513826 doi (DE-627)OLC205051218X (DE-He213)A:1008174513826-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn Breccia, Javier D. verfasserin aut Isolation of β-Xylanase from whole broth of Bacillus amyloliquefaciens by adsorption on a matrix in fluidized bed with low degree of expansion 1999 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Kluwer Academic Publishers 1999 Abstract β-1,4-Xylanase, produced extracellularly by Bacillus amyloliquefaciens MIR 32, was isolated directly from the culture broth by adsorption on a cation exchanger, Amberlite IRC-50, in fluidized bed with a low degree of expansion. The enzyme was eluted from the adsorbent by increase in pH, with a recovery of 82.3% and purification of 5.3 fold. About 99.99% of the colony forming units, 82% of the contaminating neutral protease activity, and 100% of the reducing sugars present in the crude feedstock were removed at the end of the purification cycle. Hatti-Kaul, Rajni aut Castro, Guillermo R. aut Siñeriz, Faustino aut Enthalten in Bioseparation Kluwer Academic Publishers, 1990 8(1999), 6 vom: Nov., Seite 273-280 (DE-627)130868930 (DE-600)1033272-8 (DE-576)063974134 0923-179X nnns volume:8 year:1999 number:6 month:11 pages:273-280 https://doi.org/10.1023/A:1008174513826 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_65 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_4012 AR 8 1999 6 11 273-280 |
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10.1023/A:1008174513826 doi (DE-627)OLC205051218X (DE-He213)A:1008174513826-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn Breccia, Javier D. verfasserin aut Isolation of β-Xylanase from whole broth of Bacillus amyloliquefaciens by adsorption on a matrix in fluidized bed with low degree of expansion 1999 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Kluwer Academic Publishers 1999 Abstract β-1,4-Xylanase, produced extracellularly by Bacillus amyloliquefaciens MIR 32, was isolated directly from the culture broth by adsorption on a cation exchanger, Amberlite IRC-50, in fluidized bed with a low degree of expansion. The enzyme was eluted from the adsorbent by increase in pH, with a recovery of 82.3% and purification of 5.3 fold. About 99.99% of the colony forming units, 82% of the contaminating neutral protease activity, and 100% of the reducing sugars present in the crude feedstock were removed at the end of the purification cycle. Hatti-Kaul, Rajni aut Castro, Guillermo R. aut Siñeriz, Faustino aut Enthalten in Bioseparation Kluwer Academic Publishers, 1990 8(1999), 6 vom: Nov., Seite 273-280 (DE-627)130868930 (DE-600)1033272-8 (DE-576)063974134 0923-179X nnns volume:8 year:1999 number:6 month:11 pages:273-280 https://doi.org/10.1023/A:1008174513826 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_65 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_4012 AR 8 1999 6 11 273-280 |
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10.1023/A:1008174513826 doi (DE-627)OLC205051218X (DE-He213)A:1008174513826-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn Breccia, Javier D. verfasserin aut Isolation of β-Xylanase from whole broth of Bacillus amyloliquefaciens by adsorption on a matrix in fluidized bed with low degree of expansion 1999 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Kluwer Academic Publishers 1999 Abstract β-1,4-Xylanase, produced extracellularly by Bacillus amyloliquefaciens MIR 32, was isolated directly from the culture broth by adsorption on a cation exchanger, Amberlite IRC-50, in fluidized bed with a low degree of expansion. The enzyme was eluted from the adsorbent by increase in pH, with a recovery of 82.3% and purification of 5.3 fold. About 99.99% of the colony forming units, 82% of the contaminating neutral protease activity, and 100% of the reducing sugars present in the crude feedstock were removed at the end of the purification cycle. Hatti-Kaul, Rajni aut Castro, Guillermo R. aut Siñeriz, Faustino aut Enthalten in Bioseparation Kluwer Academic Publishers, 1990 8(1999), 6 vom: Nov., Seite 273-280 (DE-627)130868930 (DE-600)1033272-8 (DE-576)063974134 0923-179X nnns volume:8 year:1999 number:6 month:11 pages:273-280 https://doi.org/10.1023/A:1008174513826 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_65 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_4012 AR 8 1999 6 11 273-280 |
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Isolation of β-Xylanase from whole broth of Bacillus amyloliquefaciens by adsorption on a matrix in fluidized bed with low degree of expansion |
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Abstract β-1,4-Xylanase, produced extracellularly by Bacillus amyloliquefaciens MIR 32, was isolated directly from the culture broth by adsorption on a cation exchanger, Amberlite IRC-50, in fluidized bed with a low degree of expansion. The enzyme was eluted from the adsorbent by increase in pH, with a recovery of 82.3% and purification of 5.3 fold. About 99.99% of the colony forming units, 82% of the contaminating neutral protease activity, and 100% of the reducing sugars present in the crude feedstock were removed at the end of the purification cycle. © Kluwer Academic Publishers 1999 |
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Abstract β-1,4-Xylanase, produced extracellularly by Bacillus amyloliquefaciens MIR 32, was isolated directly from the culture broth by adsorption on a cation exchanger, Amberlite IRC-50, in fluidized bed with a low degree of expansion. The enzyme was eluted from the adsorbent by increase in pH, with a recovery of 82.3% and purification of 5.3 fold. About 99.99% of the colony forming units, 82% of the contaminating neutral protease activity, and 100% of the reducing sugars present in the crude feedstock were removed at the end of the purification cycle. © Kluwer Academic Publishers 1999 |
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Abstract β-1,4-Xylanase, produced extracellularly by Bacillus amyloliquefaciens MIR 32, was isolated directly from the culture broth by adsorption on a cation exchanger, Amberlite IRC-50, in fluidized bed with a low degree of expansion. The enzyme was eluted from the adsorbent by increase in pH, with a recovery of 82.3% and purification of 5.3 fold. About 99.99% of the colony forming units, 82% of the contaminating neutral protease activity, and 100% of the reducing sugars present in the crude feedstock were removed at the end of the purification cycle. © Kluwer Academic Publishers 1999 |
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The enzyme was eluted from the adsorbent by increase in pH, with a recovery of 82.3% and purification of 5.3 fold. 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