An Attempt to Evaluate the Subsite Structure of Cycloamylose glucanotransferase from  Bacillus stearothermophilus : Based on its Transfer Reaction with Substrate Malto‐oligosaccharides | Zendy

Ohnishi Matasake | Zendy; Mitsune Tamaki | Zendy; Tabata Mihoko | Zendy; Kubota Michio | Zendy; Rokushika Souji | Zendy

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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.

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