Enzymes in Organic Synthesis VII—Enzymatic Activity of Hrp After Chemical Modification of the Carbohydrate Moiety
- 1 January 1990
- journal article
- research article
- Published by Taylor & Francis in Biocatalysis
- Vol. 3 (3) , 227-233
- https://doi.org/10.3109/10242429008992065
Abstract
The carbohydrate moiety of horseradish peroxidase was conjugated with hexadecylamine or octylamine in a micellar medium. Recovery and purification of these conjugates was facilitated by the short length of the added spacers. The modification increased the liposolubility of the enzyme without detracting from its catalytic activity. For the hexadecylamine conjugate, the optimum reaction temperature was increased by 10d`C. In addition, activity in organic solvents, such as toluene or chloroform, remained high, even at 70d`C.Keywords
This publication has 7 references indexed in Scilit:
- Synthesis by Enzymatic Catalysis VI—An Investigation of Chemical Modification of HRP by Fourier Transform Infra-Red Vibrational SpectroscopyBiocatalysis, 1990
- Biocatalysis in Organic Solvents with a Polymer-Bound Horseradish PeroxidaseBiocatalysis, 1989
- Application of the reaction of dithioesters with ε-amino groups in lysine to the chemical modification of proteinsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Aspects Of Biocatalyst Stability In Organic SolventsBiocatalysis, 1987
- Acidities and Basicities in Reversed Micellar SystemsPublished by Springer Nature ,1984
- A new approach to preparative enzymatic synthesisBiotechnology & Bioengineering, 1977
- 6-Substituted s-triazolo[4,3-b]-s-tetrazine-3-thiols: a sensitive and specific test for aldehydesJournal of the Chemical Society, Perkin Transactions 1, 1975