Binding of Tris to Bacillus licheniformis alpha-amylase can affect its starch hydrolysis activity.
Bacillus licheniformis alpha-amylase (BLA) is routinely used as a model thermostable amylase in biochemical studies. Its starch hydrolysis activity has recently been studied in Tris buffer. Here, we address the question that whether the application of Tris buffer may influence the results of BLA activity analyses. Based on the inhibition studies and docking simulations, we suggest that Tris molecule is a competitive inhibitor of starch-hydrolyzing activity of BLA, and it has a high tendency to bind the enzyme active site. Hence, it is critically important to consider such effect when interpreting the results of activity studies of this enzyme in Tris buffer.
Ghalanbor
Zahra
Z
University of Tehran, Tehran, Iran.
Ghaemi
Nasser
N
Marashi
Sayed-Amir
SA
Amanlou
Massoud
M
Habibi-Rezaei
Mehran
M
Khajeh
Khosro
K
Ranjbar
Bijan
B
D001665:Binding Sites; D002021:Buffers; D003198:Computer Simulation; D006868:Hydrolysis; D008958:Models, Molecular; D013213:Starch / Q000378:metabolism*; D014325:Tromethamine / Q000378:metabolism*; D000516:alpha-Amylases / Q000037:antagonists & inhibitors / Q000378:metabolism
D002021:Buffers; D014325:Tromethamine; D013213:Starch; D000516:alpha-Amylases; C501919:alpha-amylase, Bacillus licheniformis