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International Journal of Biological Macromolecules
Article . 2020 . Peer-reviewed
License: Elsevier TDM
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Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase

Authors: Božić, Nataša; Rozeboom, Henriëtte J.; Lončar, Nikola; Šokarda Slavić, Marinela; Janssen, Dick B.; Vujčić, Zoran;

Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase

Abstract

α-Amylase from Bacillus paralicheniformis (BliAmy), belonging to GH13_5 subfamily of glycoside hydrolases, was proven to be a highly efficient raw starch digesting enzyme. The ability of some α-amylases to hydrolyze raw starch is related to the existence of surface binding sites (SBSs) for polysaccharides that can be distant from the active site. Crystallographic studies performed on BliAmy in the apo form and of enzyme bound with different oligosaccharides and oligosaccharide precursors revealed binding of these ligands to one SBS with two amino acids F257 and Y358 mainly involved in complex formation. The role of this SBS in starch binding and degradation was probed by designing enzyme variants mutated in this region (F257A and Y358A). Kinetic studies with different substrates show that starch binding through the SBS is disrupted in the mutants and that F257 and Y358 contributed cumulatively to binding and hydrolysis. Mutation of both sites (F257A/Y358A) resulted in a 5-fold lower efficacy with raw starch as substrate and at least 5.5-fold weaker binding compared to the wild type BliAmy, suggesting that the ability of BliAmy to hydrolyze raw starch with high efficiency is related to the level of its adsorption onto starch granules.

This is the peer-reviewed version of the article: N. Božić, H.J. Rozeboom, N. Lončar, et al., Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase, International Journal of Biological Macromolecules, 2020, 165, A, 1529-1539, DOI: [https://doi.org/10.1016/j.ijbiomac.2020.10.025]

Published version: [https://cer.ihtm.bg.ac.rs/handle/123456789/3728]

Countries
Serbia, Netherlands, Serbia
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Subjects by Vocabulary

Microsoft Academic Graph classification: Starch Polysaccharide Hydrolysis chemistry.chemical_compound Glycoside hydrolase Amylase chemistry.chemical_classification biology Active site Oligosaccharide Biochemistry chemistry biology.protein Starch binding

Keywords

OLIGOSACCHARIDE, Glycoside Hydrolases, Surface Properties, Surface binding site, CRYSTALLOGRAPHIC ANALYSES, Oligosaccharides, Bacillus, Biochemistry, Substrate Specificity, Structural Biology, Catalytic Domain, ACARBOSE, α-Amylase, CRYSTAL-STRUCTURE, Molecular Biology, Binding Sites, RAW-STARCH, Crystal structure, Hydrolysis, Mutant, MALTOHEXAOSE-PRODUCING AMYLASE, GLUCOAMYLASE, Starch, General Medicine, DOMAIN-C, SUBSTRATE COMPLEX, Kinetics, alpha-Amylases

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
views
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