Stability of invertase in reverse micelles
Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology, ISSN: 0273-2289, Vol: 60, Issue: 1, Page: 33-39
1996
- 12Citations
- 7Captures
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Article Description
The stability of invertase was studied under various conditions, including at 75°C, in presence of stabilizers (sorbitol and glycerol) at 75°C, and in the presence of denaturants (urea and trichloroacetic acid) at 37°C in reverse micelles. Stability of the invertase in reverse micelles was found to be improved over that of the enzyme in bulk aqueous solution. Sorbitol could enhance enzyme stability as it does in the bulk aqueous system. The stabilizing effect of glycerol was reduced in reverse micelles. The denaturation pattern of urea remains unaltered. However, the denaturation effect of trichloroacetic acid has been reduced in reverse micelles. ©Copyright 1996 by Humana Press Inc. All rights of any nature whatsoever reserved.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0030187715&origin=inward; http://dx.doi.org/10.1007/bf02788057; http://www.ncbi.nlm.nih.gov/pubmed/8756613; http://link.springer.com/10.1007/BF02788057; http://www.springerlink.com/index/pdf/10.1007/BF02788057; https://dx.doi.org/10.1007/bf02788057; https://link.springer.com/article/10.1007/BF02788057; http://www.springerlink.com/index/10.1007/BF02788057
Springer Science and Business Media LLC
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