Sustrate-specificity of glucomylase (E.C. 3.2.1.3) exemplified by p-nitroaniline n-glucosides

Kossobudzki, L.

Archivum Immunologiae et Therapiae Experimentalis 24(6): 935-954

1976


ISSN/ISBN: 0004-069X
PMID: 13765
Document Number: 99990
The present paper supplements the previous investigations on the mechanism of reactions catalyzed by amylolytic enzymes. The performed experiments corroborated the data on transglucosylative properties of animal glucoamylases which were found to depend on the structure and concentration of substrate. The p-nitroanilines were first introduced in this type of research enabling to find the differences of activity mechanism of animal glucoamylases and Aspergillus niger glucoamylase. In complement to the data reported by Japanese students the transglucosylative properties of glucoamylases were shown to depend not only on the enzyme origin and substrate concentration but also on the chemical composition of applied substrate and concentration of hydrogen ions in the reaction medium.

Document emailed within 1 workday
Secure & encrypted payments