Thermostable α-amylase immobilization: Enhanced stability and performance for starch biocatalysis
| Autor: | Chandrasekhar Gurramkonda, Gudi Satheesh Kumar, Bontha Rajasekhar Reddy, Gulam M. Rather |
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| Rok vydání: | 2015 |
| Předmět: |
0301 basic medicine
Calcium alginate Immobilized enzyme Starch Biomedical Engineering Bioengineering 02 engineering and technology Applied Microbiology and Biotechnology 03 medical and health sciences Hydrolysis chemistry.chemical_compound Drug Discovery Amylase Response surface methodology Chromatography biology Process Chemistry and Technology Substrate (chemistry) General Medicine 021001 nanoscience & nanotechnology 030104 developmental biology chemistry Biochemistry Biocatalysis biology.protein Molecular Medicine 0210 nano-technology Biotechnology |
| Zdroj: | Biotechnology and Applied Biochemistry. 63:57-66 |
| ISSN: | 0885-4513 |
| DOI: | 10.1002/bab.1350 |
| Popis: | The uses of thermostable starch hydrolytic biocatalysts are steadily increasing for the industrial application because of their obvious need for biocatalytic performance at elevated temperatures. The starch liquefaction and saccharification can be carried out simultaneously by the use of thermostable starch hydrolytic biocatalysts, thus minimizing the unit operations, time, and efforts. The cost factor hampers the industrialization of expensive soluble (free) enzymes for biocatalytic applications and the immobilization of enzymes offers promising alternative to the hurdle. The present investigation was aimed for immobilization of thermostable α-amylase using calcium alginate, and statistical optimization studies were carried out for enhanced biocatalytic performance. Initially, one-parameter at a time optimization studies were carried out for identification of significant factors influencing the immobilization. Furthermore, a statistical approach, response surface methodology, was applied for immobilization of α-amylase. The immobilized α-amylase in alginate microbeads showed enhanced stability to temperature and reusable property for up to seven cycles (with the retention of 50% initial activity). Finally, the kinetic behavior of free and immobilized enzyme showed the Km value of 1.2% and 2.6% (w/v) and Vmax of 1,020 and 1,030 U, respectively. Fifty percent reduction in affinity of the immobilized enzyme toward substrate was compensated by its longer stability. |
| Databáze: | OpenAIRE |
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