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An Attempt to Evaluate the Subsite Structure of Cycloamylose glucanotransferase from Bacillus stearothermophilus : Based on its Transfer Reaction with Substrate Malto‐oligosaccharides
Author(s) -
Ohnishi Matasake,
Mitsune Tamaki,
Tabata Mihoko,
Kubota Michio,
Rokushika Souji
Publication year - 1997
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.19970490907
Subject(s) - substrate (aquarium) , bacillus (shape) , chemistry , chromatography , degradation (telecommunications) , function (biology) , stereochemistry , combinatorial chemistry , biology , microbiology and biotechnology , computer science , ecology , telecommunications , evolutionary biology
Based on determination of the transferred products (maltooligosaccharides G n ), the plausible degradation modes of G 2 , G 3 , and G 4 were analyzed quantitatively, and it was made an attempt to evaluate the binding affinity A i on some subsites of cycloamylose glucanotransferase (CGT) from Bacillus stearothermophilus . This method can be employed instead of the technique using a radioisotope. The quantities of the substrates (G 2 –G 4 ) and products G n were measured by using the HPLC techniques as a function fo time for the CGT‐catalysed reaction.