Binding of Tris to Bacillus licheniformis α-Amylase Can Affect Its Starch Hydrolysis Activity

Author(s): Zahra Ghalanbor, Nasser Ghaemi, Sayed-Amir Marashi, Massoud Amanlou, Mehran Habibi-Rezaei, Khosro Khajeh, Bijan Ranjbar, Yau Sang Chan, Jack Ho Wong, Tzi Bun Ng.

Journal Name: Protein & Peptide Letters

Volume 15 , Issue 2 , 2008


Bacillus licheniformis α-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.

Keywords: BLA, Tris inhibition, buffer inhibition, activity, docking, French bean, glucuronic acid, lectin, mitogenic activity, HepG2, breast cancer, glycoproteins, N-acetylgalactosamine-binding, polysaccharides, inflammation,, thrombosis, metastasis, Phaseolus vulgaris, AKTA Purifier, PBS, SDS-PAGE, HPLC, MCF7, CNE1, CNE2, MTT, Affi-gel blue gel, FPLC, hemagglutinating, N-acetylglucosamine, Aprotinin, Ovalbumin, Temperature, CNE, PHAs, ATP, Con A, chromatography, gel filtration, anti-HIV reverse transcriptase

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Article Details

Year: 2008
Page: [212 - 214]
Pages: 3
DOI: 10.2174/092986608783489616
Price: $58

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