Immobilization of α-amylase from Bacillus circulans GRS 313 on coconut fiber
A simple and inexpensive method for immobilizing α-amylase from Bacillus circulans GRS 313 on conconut fiber was developed. The immobilization conditions for highest efficiency were optimized with respect to immobilization pH of 5.5, 30°C, contact time of 4 h, and enzyme to support a ratio of 1:1 containing 0.12 mg/mL of protein. The catalytic properties of the immobilized enzyme were compared with that of the free enzyme. The activity of amylase adsorbed on coconut fiber was 38.7 U/g of fiber at its optimum pH of 5.7 and 48°C, compared with the maximum activity of 40.2 U/mL of free enzyme at the optimum pH of 4.9 and 48°C. The reutilization capacity of the immobilized enzyme was up to three cycles.
Index EntriesCoconut fiber adsorption response surface methodology amylase Bacillus circulans GRS 313
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- 4.Murao, S., Inui, M., and Arai, M. (1977), Hakko Kogaku Kaishi 55, 75–77.Google Scholar
- 8.Konduru, S., Evans, M. R., and Stamps, R. H. (1999), Hort. Sci. 34, 1–4.Google Scholar
- 12.Khuri, A. L. and Cornell, J. A. (1987), Statistics: Textbooks and Monographs, Marcell Dekker, New York.Google Scholar
- 13.Bernath, F. R. and Vieth, W. R. (1974), Immobilized Enzymes in Food and Microbial Processes, Plenum, New York.Google Scholar
- 15.Lartigue, D. J. (1975), Immobilized Enzymes for Industrial Reactors, Academic, New York.Google Scholar
- 16.Sunitha, J. and Sai Prakash, P. K. (1994), Ind. J. Biochem. Biophys. 31, 486–489.Google Scholar