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Removal of the four C-terminal glycine rich repeats enhances the thermostability of barley β-amylase
journal contribution
posted on 2023-05-16, 16:32 authored by Ma, YF, Eglinton, JK, Evans, E, Logue, SJ, Langridge, PBarley β-amylase undergoes proteolytic cleavage in the C-terminal region after germination. The implication of the cleavage in the enzyme's characteristics is unclear. With purified native β-amylases from both mature barley grain and germinated barley, we found that the β-amylase from germinated barley had significantly higher thermostability and substrate binding affinity for starch than that from mature barley grain. To better understand the effect of the proteolytic cleavage on the enzyme's thermostability and substrate binding affinity for starch, recombinant barley β-amylases with specific deletions at the C-terminal tail were generated. The complete deletion of the four C-terminal glycine-rich repeats significantly increased the enzyme's thermostability, but an incomplete deletion with one repeat remaining did not change the thermostability. Although different C-terminal deletions affect the thermostability differently, they all increased the enzyme's affinity for starch. The possible reasons for the increased thermostability and substrate binding affinity, due to the removal of the four C-terminal glycine-rich repeats, are discussed in terms of the three-dimensional structure of β-amylase.
History
Publication title
BiochemistryVolume
39Pagination
13350-13355ISSN
0006-2960Department/School
Tasmanian Institute of Agriculture (TIA)Publisher
American Chemical SocietyPlace of publication
United StatesRepository Status
- Restricted