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Published on: September 20, 2016
Xylanase inhibitors bind to nonstarch polysaccharides
Ellen Fierens1, Kurt Gebruers, Christophe M Courtin
1Laboratory of Food Chemistry and Biochemistry, Department of Microbial and Molecular Systems, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, Box 2463, 3001 Leuven, Belgium. ellen.fierens@biw.kuleuven.be
Wheat xylanase inhibitors (TAXI, XIP, TLXI) bind to beta-glucans and arabinoxylans. Their binding affinity for arabinoxylans increases as the arabinose/xylose ratio decreases.
Area of Science:
- Plant biochemistry
- Food science
- Enzyme inhibition
Background:
- Xylanase inhibitors are proteins found in cereals like wheat.
- These inhibitors play a role in plant defense and can affect food processing.
- Understanding their interactions with polysaccharides is crucial for biotechnological applications.
Purpose of the Study:
- To investigate the binding interactions between wheat xylanase inhibitors (TAXI, XIP, TLXI) and various polysaccharides.
- To determine how polysaccharide structure, specifically the arabinose/xylose ratio and solubility, affects inhibitor binding.
- To elucidate the natural function of xylanase inhibitors and their impact on cereal-based processes.
Main Methods:
- Incubation of xylanase inhibitors (TAXI, XIP, TLXI) with different beta-glucans and (arabino)xylans.
- Measurement of residual xylanase inhibition activity to assess binding affinity.
- Analysis of the effect of varying arabinose/xylose ratios and polysaccharide solubility (water-extractable vs. water-unextractable) on inhibitor binding.
Main Results:
- All three wheat xylanase inhibitors (TAXI, XIP, TLXI) demonstrated binding to both beta-glucans and (arabino)xylans.
- Binding affinity for (arabino)xylans increased significantly with a lower arabinose/xylose ratio.
- This interaction was observed irrespective of whether the (arabino)xylans were water-extractable or water-unextractable.
Conclusions:
- Wheat xylanase inhibitors interact with diverse polysaccharides, including beta-glucans and (arabino)xylans.
- The structural characteristics of (arabino)xylans, particularly the arabinose/xylose ratio, are key determinants of inhibitor binding.
- These findings enhance our understanding of xylanase inhibitor function in nature and their potential effects in cereal biotechnology, such as bread making.
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