Synthesis by Enzymatic Catalysis VI—An Investigation of Chemical Modification of HRP by Fourier Transform Infra-Red Vibrational Spectroscopy

Arseguel, Didier; Lattes, Armand; Baboulène, M.

doi:10.3109/10242429008992064

Search citation statements

Order By: Relevance

Paper Sections

Select...

Introduction1

Citation Types

Supporting

Mentioning

Contrasting

Year Published

1990

1994

Publication Types

Select...

Article2

Relationship

Self Cite1

Independent1

Authors

Journals

Cited by 2 publications

(1 citation statement)

References 5 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A considerable body of research has therefore been devoted to the optimization of enzyme reactions (Lunblad and Noyes, 1984) by employing biphasic (Klibanov et al, 1977) or micellar media (Bunton, 1976). Horseradish peroxidase or HRP (EC 1.11.1.7) is an oxido-reductase with considerable industrial potential (Seris, 1985) since it can accept a wide range of aromatic substrates.…”

Section: Introductionmentioning

confidence: 99%

Enzymes in Organic Synthesis VII—Enzymatic Activity of Hrp After Chemical Modification of the Carbohydrate Moiety

1990

Self Cite

View full text Add to dashboard Cite

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 10°C. In addition, activity in organic solvents, such as toluene or chloroform, remained high, even at 70°C.

show abstract

Section: Introductionmentioning

confidence: 99%