Premium
Untersuchung der Kinetik der Amylolyse
Author(s) -
Holló J.,
Làszló E.
Publication year - 1971
Publication title -
starch ‐ stärke
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.62
H-Index - 82
eISSN - 1521-379X
pISSN - 0038-9056
DOI - 10.1002/star.19710230804
Subject(s) - pyranose , hydrolysis , chemistry , starch , substrate (aquarium) , kinetics , hydrogen bond , molecule , ring (chemistry) , amylase , crystallography , enzymatic hydrolysis , enzyme , stereochemistry , organic chemistry , physics , biology , quantum mechanics , ecology
Examination of the Kinetics of Amylolysis. A new theory to explain the extraordinarily strong effectiveness of enzymatic hydrolysis has been developed from the kinetic data on the starch hydrolysis catalyzed by acid or respectively by ß‐amylase. According to this theory the ß‐amylase gradually fits itself to the substrate of spiral structure. This adaption induces the development of hydrogen bonds formed in stages between side chains of the enzyme molecule. By this development the space structure of the bond to be split up or the pyranose ring is several times more easily attacked and split up as it is the case with non‐deformed structure.