Production of alkaline protease with immobilized cells of bacillus subtilis PE-11 in various matrices by entrapment technique
Autor: | Poluri Ellaiah, Bezawada Jyothi, K. Adinarayana |
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Jazyk: | angličtina |
Rok vydání: | 2005 |
Předmět: |
Calcium alginate
food.ingredient Alginates Polyacrylamide Pharmaceutical Science Bacillus subtilis Aquatic Science Gelatin Article chemistry.chemical_compound food Bacterial Proteins Glucuronic Acid Drug Discovery Endopeptidases Technology Pharmaceutical Subtilisins Ecology Evolution Behavior and Systematics chemistry.chemical_classification Chromatography Ecology biology Chemistry Hexuronic Acids Alkaline protease General Medicine Glucuronic acid biology.organism_classification Enzyme Biochemistry Fermentation Agronomy and Crop Science |
Popis: | The purpose of this investigation was to study the effect of Bacillus subtilis PE-11 cells immobilized in various matrices, such as calcium alginate, k-Carrageenan, ployacrylamide, agar-agar, and gelatin, for the production of alkaline protease. Calcium alginate was found to be an effective and suitable matrix for higher alkaline protease productivity compared to the other matrices studied. All the matrices were selected for repeated batch fermentation. The average specific volumetric productivity with calcium alginate was 15.11 U/mL/hour, which was 79.03% higher production over the conventional free-cell fermentation. Similarly, the specific volumetric productivity by repeated batch fermentation was 13.68 U/mL/hour with k-Carrageenan, 12.44 U/mL/hour with agar-agar, 11.71 U/mL/hour with polyacrylamide, and 10.32 U/mL/hour with gelatin. In the repeated batch fermentations of the shake flasks, an optimum level of enzyme was maintained for 9 days using calcium alginate immobilized cells. From the results, it is concluded that the immobilized cells of B subtilis PE-11 in calcium alginate are more efficient for the production of alkaline protease with repeated batch fermentation. The alginate immobilized cells of B subtilis PE-11 can be proposed as an effective biocatalyst for repeated usage for maximum production of alkaline protease. |
Databáze: | OpenAIRE |
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