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Cold-active winter rye glucanases with ice-binding capacity.

Mahmoud W F Yaish1, Andrew C Doxey, Brendan J McConkey

  • 1Department of Biology, University of Waterloo, Waterloo, Ontario, Canada N2L 3G1. myaish@uoguelph.ca

Plant Physiology
|July 4, 2006
PubMed
Summary

Winter rye (Secale cereale) glucanases exhibit antifreeze properties, protecting against cold damage. These cold-active enzymes inhibit ice crystal growth and may help plants survive freezing temperatures.

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Area of Science:

  • Plant molecular biology
  • Biochemistry
  • Cryobiology

Background:

  • Winter rye (Secale cereale) produces extracellular pathogenesis-related proteins, including glucanases, at cold temperatures.
  • These cold-induced glucanases possess antifreeze activity, suggesting a role in cold tolerance.

Purpose of the Study:

  • To characterize recombinant cold-induced glucanases from winter rye.
  • To investigate their hydrolytic and antifreeze activities in vitro.
  • To understand their contribution to plant cold tolerance.

Main Methods:

  • Expression of basic beta-1,3-glucanases and acidic beta-1,3;1,4-glucanase in Escherichia coli.
  • Purification and in vitro assays for hydrolytic and antifreeze activities.
  • Development of structural models to identify putative ice-binding surfaces (IBSs).

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Main Results:

  • All characterized glucanases were cold active, retaining partial hydrolytic activity at subzero temperatures.
  • Glucanases demonstrated antifreeze activity by modifying ice crystal growth.
  • Structural analysis revealed charge conservation on IBSs, with one exception correlating to reduced antifreeze activity.

Conclusions:

  • Winter rye glucanases have evolved to inhibit ice crystal formation, contributing to cold tolerance.
  • Enzymatic activity may also confer resistance to psychrophilic pathogens.
  • These proteins exemplify adaptation to cold and freezing conditions.