Citation
Nadiah Syuhada Abd Samad, . and Azura Amid, . and Dzun Noraini Jimat, . and Nurul Aqilah Ab. Shukor, . Protease purification from Bacillus amyloliquefaciens B7 using aqueous two-phase system (ATPS). S292-S297. ISSN 2231-7546
Abstract
Bacillus amyloliquefaciens B7 was isolated from the fermented fish sauce and identified as protease producer. Generally in downstream processing purification of enzymes consumes higher cost regarding reagents and equipment used. Moreover harsh purification methods used might cause denaturation of the enzymes. Therefore there is a high demand for efficient and low cost extraction and purification methods. Aqueous two-phase system (ATPS) is an alternative method that should be considered as it is simple rapid separation yet cause little denaturation. Protease produced by B. amyloliquefaciens B7 was partitioned using two different ATPS which were PEG/potassium phosphate and PEG/sodium citrate. Results showed the highest enzyme activity was found in interface phase with the ATPS system of 27 (w/w) PEG1500/34 (w/w) sodium citrate. Later the ATPS conditions (pH temperature the concentration of selected salt and PEG) were optimized by using response surface methodology. The optimum conditions for ATPS purification were observed in ATPS conditions at pH 7 and 35C with the enzyme activity of 0.20 0.01 U/ml.
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Abstract
Bacillus amyloliquefaciens B7 was isolated from the fermented fish sauce and identified as protease producer. Generally in downstream processing purification of enzymes consumes higher cost regarding reagents and equipment used. Moreover harsh purification methods used might cause denaturation of the enzymes. Therefore there is a high demand for efficient and low cost extraction and purification methods. Aqueous two-phase system (ATPS) is an alternative method that should be considered as it is simple rapid separation yet cause little denaturation. Protease produced by B. amyloliquefaciens B7 was partitioned using two different ATPS which were PEG/potassium phosphate and PEG/sodium citrate. Results showed the highest enzyme activity was found in interface phase with the ATPS system of 27 (w/w) PEG1500/34 (w/w) sodium citrate. Later the ATPS conditions (pH temperature the concentration of selected salt and PEG) were optimized by using response surface methodology. The optimum conditions for ATPS purification were observed in ATPS conditions at pH 7 and 35C with the enzyme activity of 0.20 0.01 U/ml.
Additional Metadata
| Item Type: | Article |
|---|---|
| AGROVOC Term: | Bacillus |
| AGROVOC Term: | Proteases |
| AGROVOC Term: | Alternative methods |
| AGROVOC Term: | Condiments |
| AGROVOC Term: | Purification |
| AGROVOC Term: | Denaturation |
| AGROVOC Term: | Enzymes |
| AGROVOC Term: | Enzyme activity |
| AGROVOC Term: | Sodium |
| AGROVOC Term: | Potassium |
| Depositing User: | Ms. Suzila Mohamad Kasim |
| Last Modified: | 24 Apr 2025 06:28 |
| URI: | http://webagris.upm.edu.my/id/eprint/23945 |
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